The Wüthrich Laboratory

Kurt Wüthrich: Complete List of Publications

1. Wüthrich, K. und Fallab, S. (1963) Chimia 17, 356–358.
Bestimmung der Bildungskonstanten der o-Phenylendiamin-Kupfer(II)-Komplexe in wässriger Lösung.

2. Wüthrich, K. und Fallab, S. (1964) Helv. Chim. Acta 47, 1440–1448.
Mechanismus der Kupfer(II)-katalysierten Autoxydation von o-Phenylendiamin.

3. Wüthrich, K. und Fallab, S. (1964) Helv. Chim. Acta 47, 1609–1616.
Einfluss verschiedener Liganden auf den Mechanismus der Kupfer(II)-katalysierten Autoxydation von o-Phenylendiamin.

4. Wüthrich, K., Loeliger, H. und Fallab, S. (1964) Experientia 20, 599–601.
Elektronenspinresonanzmessungen zur Untersuchung von Kinetik und Mechanismus von Cu²⁺-katalysierten Reaktionen.

5. Wüthrich, K. (1965) Helv. Chim. Acta 48, 779–790.
Elektronenspinresonanz-Untersuchungen von VO²⁺-Komplexverbindungen in wässeriger Lösung.

6. Wüthrich, K. (1965) Helv. Chim. Acta 48, 1012–1017.
Elektronenspinresonanz-Untersuchungen von VO²⁺-Komplexverbindungen in wässeriger Lösung II.

7. Wüthrich, K. (1966) Helv. Chim. Acta 49, 1400–1406.
Über die Elektronenspinresonanzspektren einiger Cu²⁺-Komplexe in wässeriger Lösung.

8. Wüthrich, K. and Connick, R.E. (1967) Inorg. Chem. 6, 583–590.
Nuclear magnetic resonance relaxation of oxygen-17 in aqueous solutions of vanadyl perchlorate and the rate of elimination of water molecules from the first coordination sphere.

9. Wüthrich, K., Shulman, R.G. and Peisach, J. (1968) Proc. Natl. Acad. Sci. USA 60, 373–380.
High resolution proton magnetic resonance spectra of sperm whale cyanometmyoglobin.

10. Wüthrich, K. and Connick, R.E. (1968) Inorg. Chem. 7, 1377–1388.
Nuclear magnetic resonance studies of the coordination of vanadyl complexes in solution and the rate of elimination of coordinated water molecules.

11. Wüthrich, K., Shulman, R.G. and Yamane, T. (1968) Proc. Natl. Acad. Sci. USA 61, 1199–206.
Proton magnetic resonance studies of human cyanomethemoglobin.

12. Wüthrich, K., Shulman, R.G., Wyluda, B.J. and Caughey, W.S. (1969) Proc. Natl. Acad. Sci. USA 62, 636–643.
Proton magnetic resonance studies of porphyrin iron(III) cyanides.

13. Shulman, R.G., Ogawa, S., Wüthrich, K., Yamane, T., Peisach, J. and Blumberg, W.E. (1969) Science 165, 251–257.
The absence of “heme–heme” interactions in hemoglobin.

14. Shulman, R.G., Wüthrich, Yamane, T., Antonini, E. and Brunori, M. (1969) Proc. Natl. Acad. Sci. USA 63, 623–628.
Nuclear magnetic resonances of reconstituted myoglobins.

15. Wüthrich, K. (1969) Proc. Natl. Acad. Sci. USA 63, 1071–1078.
High resolution proton nuclear magnetic resonance spectroscopy of cytochrome c.

16. Connick, R.E. and Wüthrich, K. (1969) J. Chem. Phys. 51, 4506–4508.
¹⁷O nuclear magnetic relaxation in aqueous solutions of diamagnetic metal ions.

17. Wüthrich, K., Meiboom, S. and Snyder, L.C. (1970) J. Chem. Phys. 52, 230–233.
Nuclear magnetic resonance spectroscopy of bicyclobutane.

18. Wüthrich, K. and Shulman, R.G. (1970) Physics Today 23, 43–50.
Magnetic resonance in biology.

19. Yamane, T., Wüthrich, K., Shulman, R.G. and Ogawa, S. (1970) J. Mol. Biol. 49, 197–202.
Proton magnetic resonance studies of cyanoferrihemoglobins from different species.

20. Wüthrich, K., Shulman, R.G., Yamane, T., Wyluda, B.J., Hügli , B.J. and Gurd, F.R.N. (1970) J.Biol. Chem. 245, 1947–1953.
High resolution proton magnetic resonance studies of cyanoferrimyoglobins and alkylated derivatives from different species.

21. Shulman, R.G., Wüthrich, K., Yamane, T., Patel, D.J. and Blumberg, W.E. (1970) J. Mol. Biol. 53, 143–157.
Nuclear magnetic resonance determination of ligand-induced conformational changes in myoglobin.

22. Wüthrich, K. (1970) Structure and Bonding 8, 53–121.
Structural studies of hemes and hemoproteins by nuclear magnetic resonance spectroscopy.

23. Wüthrich, K. (1970) Chimia 24, 409–418.
Studien der räumlichen Struktur von Proteinmolekülen mit magnetischer Kernresonanzspek-troskopie.

24. Shulman, R.G., Ogawa, S., Wüthrich, K., Yamane, T., Peisach, J. and Blumberg, W.E. (1970) in Physical Problems in Biological Systems, (C.de Witt and J. Matricon, eds.) pp. 235–249, Gordon and Breach, New York.
The absence of “heme-heme” interactions in hemoglobin.

25. Wüthrich, K. (1970) dans Physique et Chimie, Numéro Spécial Annuel 1970: La Biophysique, pp. 18–25, Editions de l’Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris.
Structures électroniques dans les hémoprotéines: études par résonance magnétique nucléaire.

26. Wüthrich, K., Meraldi, J.P., Tun-Kyi, A. and Schwyzer, R. (1971) in Proc. 1st Eur. Biophysics Congress, Vol. I, pp. 93–95, Verlag der Wiener Medizinischen Akademie.
Structural studies by nuclear magnetic resonance of a cationspecific peptide.

27. Shulman, R.G., Wüthrich, K. and Peisach, J. (1971) in Probes of Structure and Function of Macromolecules and Membranes, Vol. II: Probes of Enzymes and Hemoproteins(B. Chance, T.Yonetani and A.S. Mildvan, eds.) pp. 195–204, Academic Press, New York.
High resolution proton magnetic resonance studies of myoglobin.

28. Wüthrich, K. (1971) in Probes of Structure and Function of Macromolecules and Membranes, Vol. II: Probes of Enzymes and Hemoproteins (B. Chance, T. Yonetani and A.S. Mildvan, eds.) pp. 465–486, Academic Press, New York.
High resolution proton NMR studies of the coordination of the heme iron in cytochrome c.

29. Wüthrich, K., Aviram, I. and Schejter, A. (1971) Biochim. Biophys. Acta 253, 98–103.
Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy.

30. Ogawa, S., Shulman, R.G., Wüthrich, K. and Yamane, T. (1971) in Magnetic Resonances in Biological Research (C. Franconi, ed.) pp. 97–106, Gordon and Breach, New York.
NMR studies of the role of the heme group during the cooperative oxygenation of hemoglobin.

31. Wüthrich, K., Shulman, R.G., Yamane, T. and Ogawa, S. (1971) in Genetical, Functional and Physical Studies of Hemoglobins (T. Arends, G. Bemski and R.L. Nagel, eds.) pp. 73–79, Karger, Basel.
Studies of structure–function correlations in hemoglobin by nuclear magnetic resonance.

32. Winterhalter, K.H. and Wüthrich, K. (1972) J. Mol. Biol. 63, 477–482.
Structural investigations of modified haemoglobins by nuclear magnetic resonance spectroscopy.

33. Keller, R.M., Aviram, I., Schejter, A. and Wüthrich, K. (1972) FEBS Lett. 20, 90–92.
Evidence for pentacoordinated iron (II) in carboxymethylated cytochrome c.

34. Wüthrich, K. and Shulman, R.G. (1971) Uspekhi Fizicheskikh Nauk 105, 707–720.
Magnetic resonance in biology. (Russisch)

35. Wüthrich, K., Keller, R.M., Brunori, M., Giacometti, G., Huber, R. and Formanek, H. (1972) FEBS Lett. 21, 63–66.
Similarities of the heme environment in vertebrate and non-vertebrate oxygen-binding hemoproteins.

36. Donzel, B., Kamber, B., Wüthrich, K. and Schwyzer, R. (1972) Helv. Chim. Acta 55, 947–961.
A chiral cystine disulfide group without inherent optical activity in the long-wavelength region.

37 Keller, R.M., Wüthrich, K. and Debrunner, P.G. (1972) Proc. Natl. Acad. Sci. USA 69, 2073–2075.
Proton magnetic resonance reveals high spin iron (II) in ferrous cytochrome P450_cam from Pseudomonas putida.

38. Wüthrich, K., Tun-Kyi , A. and Schwyzer, R. (1972) FEBS Lett. 25, 104–108.
Manifestation in the ¹³C NMR spectra of two different molecular conformations of a cyclic pentapeptide.

39. Meraldi, J.P., Schwyzer, R., Tun-Kyi, A. and Wüthrich, K. (1972) Helv. Chim. Acta 55, 1962–1973.
Conformational studies of cyclic pentapeptides by proton magnetic resonance spectroscopy.

40. Schwyzer, R., Grathwohl, C., Meraldi, J.P., Tun-Kyi, A., Vogel, R. and Wüthrich, K. (1972) Helv. Chim. Acta 55, 2545–2549.
The solution conformation of cyclo-glycyl-L-prolyl-glycyl-glycyl-L-prolyl-glycyl.

41. Keller, R.M. and Wüthrich, K. (1972) Biochim. Biophys. Acta 285, 326–336.
The electronic g-tensor in cytochrome b₅ : high resolution proton magnetic resonance studies.

42. Grathwohl, C., Schwyzer, R., Tun-Kyi, A. and Wüthrich, K. (1973) FEBS Lett. 29, 271–274.
Carbon-13 NMR spectra of cyclo-glycyl-L-prolyl-glycyl-glycyl-L-prolyl- glycyl: assignment of the carbonyl resonances.

43. Wüthrich, K. (1973) in Vorträge des 9. Kolloquiums über NMR-Spektroskopie (R. Kosfeld, J.Mansfeld und P. Puhr-Westerheide, eds.) Vol. 1, pp. 71–91, Rheinisch-Westfälische Technische Hochschule Aachen.
Proton and carbon-13 NMR studies of peptides and proteins.

44. Masson, A. and Wüthrich, K. (1973) FEBS Lett. 31, 114–118.
Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor.

45. Wüthrich, K. and Baumann, R. (1973) Helv. Chim. Acta 56, 585–596.
Hyperfine shifts of the ¹³C NMR in low spin iron(III) porphyrin complexes.

46. Wüthrich, K. (1973) Naturwissenschaften 60, 221–230.
Magnetische Kernresonanzspektroskopie in der Biologischen Forschung.

47. Keller, R.M., Pettigrew, G.W. and Wüthrich, K. (1973) FEBS Lett. 36, 151–156.
Structural studies by proton NMR of cytochrome c-557 from Crithidia oncopelti.

48. Keller, R.M., Groudinsky, O. and Wüthrich, K. (1973) Biochim. Biophys. Acta 328, 233–238.
Proton magnetic resonances in cytochrome b₂ core: structural similarities with cytochrome b₅.

49. Wüthrich, K., Keller, R.M. and Baumann, R. (1973) in Dynamic Aspects of Conformation Changes in Biological Macromolecules (C. Sadron, ed.) pp. 151–163. Reidel, Dordrecht.
Proton and carbon-13 nuclear magnetic resonances in hemes and hemoproteins: new aspects for the investigation of the molecular conformations.

50. Meraldi, J.P., Moeschler, H., Schwyzer, R., Tun-Kyi, A. et Wüthrich, K. (1973) J. Physique 34, C8-41–C8-43.
Etudes de la conformation de pentapeptides cycliques par la résonance magnétique nucléaire.

51. Wüthrich, K. and Baumann, R. (1973) Ann. New York Acad. Sci 222, 709–721 (1973).
Recent developments in the investigation of the paramagnetic centers in low spin ferric hemoproteins: carbon-13 hyperfine shifts in iron porphyrin complexes.

52. Wüthrich, K. and Baumann, R. (1974) Helv. Chim. Acta 57, 336–350.
Hyperfine shifts of the ¹³C NMR in protoporphyrin IX iron(III) dicyanide and deuteroporphyrin IX iron(III) dicyanide.

53. Grathwohl , C. and Wüthrich, K. (1974) J. Magn. Reson. 13, 217–225.
Carbon-13 NMR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala- OCH₃, where X stands for the 20 common amino acids.

54. Wüthrich, K. (1974) Experientia 30, 577–585.
Nuclear magnetic resonance in protein research.

55. Wüthrich, K. (1974) Pure Appl.Chem. 37, 235–248.
Studies of the molecular conformations in proteins by ¹H and ¹³C NMR spectroscopy.

56. Wüthrich, K. and Grathwohl, C. (1974) FEBS Lett. 43, 337–340.
A novel approach for studies of the molecular conformations in flexible polypeptides.

57. Wüthrich, K. and Keller, R.M. (1973) in Symposial Papers of the IVth International Biophysics Congress, Vol. 2, pp. 722–735, Academy of Sciences of the USSR, Pushino.
Recent developments in the investigation of the paramagnetic centers in low spin ferric hemoproteins.

58. Wüthrich, K., Grathwohl, C. and Schwyzer, R. (1974) in Peptides, Polypeptides and Protein (E.R.Blout, F.A. Bovey, M. Goodman and N. Lotan, eds.) pp. 300–307, Wiley, New York. Cis, trans, and nonplanar peptide bonds in oligopeptides: ¹³C NMR studies.

59. Wüthrich, K. (1974) Pure Appl. Chem. 40, 127–139.
Carbon-13 NMR in haems and haemoproteins.

60. Grathwohl, C., Tun-Kyi, A., Bundi, A., Schwyzer, R. and Wüthrich, K. (1975) Helv. Chim. Acta 58, 415–423 .
¹H and ¹³C NMR studies of the molecular conformations of cyclo-tetraglycyl.

61. Wüthrich, K. and Wagner, G. (1975) FEBS Lett. 50, 265–268.
NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor.

62. Bundi, A., Grathwohl, C., Hochmann, J., Keller, R.M., Wagner, G. and Wüthrich, K. (1975) J.Magn. Reson. 18, 191–198.
Proton NMR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala-OCH₃, where X stands for one of the 20 common amino acids.

63. Wüthrich, K., Hochmann, J., Keller, R.M., Wagner, G., Brunori, M. and Giacometti, G. J. Magn. Reson. 19, 111–113 (1975).
¹H NMR relaxation in high spin ferrous hemoproteins.

64. Llinás, M., Wüthrich, K., Schwotzer, W. and von Philipsborn, W. (1975) Nature 257, 817–818.
¹⁵N nuclear magnetic resonance of living cells.

65. Wüthrich, K. (1975) in Proc. 10th FEBS Meeting, pp. 21–24, Federation of European Biochemical Societies.
Nuclear magnetic resonance in enzyme research.

66. Wagner, G. and Wüthrich, K. (1975) J. Magn. Reson. 20, 435–445.
Proton NMR studies of the aromatic residues in the basic pancreatic trypsin inhibitor (BPTI).

67. Wagner, G., DeMarco, A. and Wüthrich, K. (1975) J. Magn. Reson. 20, 565–569.
Convolution difference ¹H NMR spectra at 360 MHz of the basic pancreatic trypsin inhibitor.

68. Brown, L.R., DeMarco, A., Wagner, G. and Wüthrich, K. (1976) Eur. J. Biochem. 62, 103–107.
A study of the lysyl residues in the basic pancreatic trypsin inhibitor using ¹H nuclear magnetic resonance at 360 MHz.

69. Wüthrich, K. (1976) NMR in Biological Research: Peptides and Proteins. North Holland, Amsterdam.

70. Wagner, G. and Wüthrich, K. (1976) in Protides of the Biological Fluids – 23rd Colloquium (H.Peeters, ed.) pp. 189–193, Pergamon, Oxford.
¹H NMR studies of the dynamics of the solution conformation of the basic pancreatic trypsin inhibitor (BPTI).

71. Wüthrich, K., Wagner, G. and Tschesche, H. (1976) in Protides of the Biological Fluids– 23rd Colloquium (H. Peeters, ed.) pp. 201–204, Pergamon, Oxford.
Comparative ¹H NMR studies of the solution conformation of the cow colostrum trypsin inhibitor (CTI), the trypsin inhibitor of helix pomatia (HPI) and the basic pancreatic trypsin inhibitor (BPTI).

72. Keller, R.M., Groudinsky, O. and Wüthrich, K. (1976) Biochim. Biophys. Acta 427, 497– 511.
Contact-shifted resonances in the ¹H NMR spectra of cytochrome b₅: resonance identification and spin density distribution in the heme group.

73. Bundi, A., Andreatta, R., Rittel, W. and Wüthrich, K. (1976) FEBS Lett. 64, –129.
Conformational studies of the synthetic fragment 1–34 of human parathyroid hormone by NMR techniques.

74. Wagner, G., DeMarco, A. and Wüthrich, K. (1976) Biophys. Struct. Mech. 2, 139–158.
Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) I: ¹H NMR studies.

75. Hetzel, R., Wüthrich, K., Deisenhofer, J. and Huber, R. (1976) Biophys. Struct. Mech. 2, 159–180.
Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) II: semi-empirical energy calculations.

76. Wüthrich, K. (1975) in Metalloprotein Studies Utilizing Paramagnetic Effects of the Metal Ions as Probes (M. Kotani and A. Tasaki, eds.) pp. 151–179, The Taniguchi Foundation, Osaka, Japan.
The heme groups as natural NMR probes of hemoprotein conformation.

77. Möschler, H.J., Tun-Kyi, A., Meraldi, J.P., Wüthrich, K. und Schwyzer, R. (1976) Helv. Chim. Acta 59, 2196–2200.
Synthese deuterierter Derivate diastereomerer Cyclopentapeptide für die Konformationsanalyse.

78. Wüthrich, K. and DeMarco, A. (1976) Helv. Chim. Acta 59, 2228–2235.
Preferred spatial arrangement of the aromatic side chains in linear oligopeptides containing tyrosine.

79. Grathwohl, C. and Wüthrich, K. (1976) Biopolymers 15, 2025–2041.
The X–Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides.

80. Grathwohl, C. and Wüthrich, K. (1976) Biopolymers 15, 2043–2057.
NMR studies of the molecular conformations in the linear oligopeptides H–(L-Ala)_n–L-Pro–OH.

81. Keller, R.M., Wüthrich, K. and Pecht, I. (1976) FEBS Lett. 70, 180–184.
Structural studies of cytochrome c-551 by ¹H NMR spectroscopy at 360 MHz.

82. DeMarco, A. and Wüthrich, K. (1976) J. Magn. Reson. 24, 201–204.
Digital filtering with a sinusoidal window function: an alternative technique for resolution enhancement in FT NMR.

83. Wüthrich, K. and Baumann, R. (1976) Org. Magn. Reson. 8, 532–535.
¹³C spin relaxation studies of the basic pancreatic trypsin inhibitor.

84. Brown, L.R. and Wüthrich, K. (1977) Biochim. Biophys. Acta 464, 356–369.
A spin label study of lipid oxidation catalyzed by heme proteins.

85. Keller, R.M., Wüthrich, K. and Schejter, A. (1977) Biochim. Biophys. Acta 491, 409–415.
¹H NMR studies of the heme iron coordination in cytochrome c-552 from Euglena gracilis.

86. Keller, R.M. and Wüthrich, K. (1977) Biochim. Biophys. Acta 491, 416–422.
¹H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome c-552 from Euglena gracilis.

87. Bundi, A. and Wüthrich, K. (1977) FEBS Lett. 77, 11–14.
¹H NMR titration shifts of amide proton resonances in polypeptide chains.

88. Llinás, M., Meier, W. and Wüthrich, K. (1977) Biochim. Biophys. Acta 492, 1–11.
A carbon-13 spin lattice relaxation study of alumichrome at 25.1 MHz and 90.5 MHz.

89. Lauterwein, J., Wüthrich, K., Schweitz, H., Vincent, J.P. and Lazdunski, M. (1977) Biochem. Biophys. Res. Comm. 76, 1071–1078.
¹H NMR studies of a neurotoxin and a cardiotoxin from Naja mossambica mossambica: amide proton resonances.

90. Richarz, R. and Wüthrich, K. (1977) FEBS Lett. 79, 64–68.
High field ¹³C NMR studies at 90.5 MHz of the methyl groups in the basic pancreatic trypsin inhibitor.

91. Brown, L.R. and Wüthrich, K. (1977) Biochim. Biophys. Acta 468, 389–410.
NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin phosphatidylcholine vesicles.

92. Wüthrich, K. (1977) in Nuclear Magnetic Resonance in Solids (L. van Gerven, ed.) pp. 347–360, Plenum Press, New York.
NMR studies of structure and conformation in peptides and proteins.

93. Wüthrich, K. (1977) in Nuclear Magnetic Resonance in Solids (L. van Gerven, ed.) pp. 361–374, Plenum Press, New York.
NMR studies of hemoproteins.

94. Wüthrich, K., Wagner, G., Richarz, R. and DeMarco, A. (1977) in NMR in Biology, (R.A. Dwek, I.D. Campbell, R.E. Richards and R.J.P. Williams, eds.) pp. 51–62, Academic Press, New York.
Completion of X-ray structures of proteins by high resolution NMR.

95. DeMarco, A., Tschesche, H., Wagner, G. and Wüthrich, K. (1977) Biophys. Struct. Mech. 3, 303–315.
¹H NMR studies at 360 MHz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI).

96. Nagayama, K., Wüthrich, K., Bachmann, P. and Ernst, R.R. (1977) Biochem. Biophys. Res. Comm. 78, 99–105.
Two-dimensional J-resolved ¹H NMR spectroscopy of biological macromolecules.

97. Nagayama, K., Wüthrich, K., Bachmann, P. and Ernst, R.R. (1977) Naturwissenschaften 64, 581–582.
Two-dimensional NMR spectroscopy: a powerful tool for the investigation of biopolymers in solution.

98. Llinás, M. and Wüthrich, K. (1978) Biochim. Biophys. Acta 532, 29–40.
A nitrogen-15 spin–lattice relaxation study of alumichrome.

99. Keller, R.M. and Wüthrich, K. (1978) Biochim. Biophys. Acta 533, 195–208.
Assignment of the heme c resonances in the 360 MHz ¹H NMR spectra of cytochrome c.

100. DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 617–636.
Analysis of the ¹H NMR spectra of ferrichrome peptides I: the non-amide protons.

101. DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 637–650.
Analysis of the ¹H NMR spectra of ferrichrome peptides II: the amide resonances.

102. Wagner, G., Wüthrich, K. and Tschesche, H. (1978) Eur. J. Biochem. 86, 67–76.
A ¹H nuclear magnetic resonance study of the conformation and the molecular dynamics of the glycoprotein cow colostrum trypsin inhibitor.

103. Richarz, R. and Wüthrich, K. (1978) J. Magn. Reson. 30, 147–150.
NOE difference spectroscopy: a novel method for observing individual multiplets in proton nmr spectra of biological macromolecules.

104. Brown, L.R., DeMarco, A., Richarz, R., Wagner, G. and Wüthrich, K. (1978) Eur. J. Biochem. 88, 87–95.
The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor: ¹H and ¹³C nuclear magnetic resonance studies of the native and the transaminated inhibitor.

105. Wüthrich, K., Wagner, G., Richarz, R. and Perkins, S.J. (1978) Biochemistry 17, 2253–2263.
Individual assignments of the methyl resonances in the ¹H nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor.

106. Richarz, R. and Wüthrich, K. (1978) Biochemistry 17, 2263–2269.
High field ¹³C nuclear magnetic resonance studies at 90.5 MHz of the basic pancreatic trypsin inhibitor.

107. Nagayama, K., Bachmann, P., Wüthrich, K. and Ernst, R.R. (1978) J. Magn. Reson. 31, 133–148.
The use of cross sections and of projections in two-dimensional NMR spectroscopy.

108. Keller, R.M. and Wüthrich, K. (1978) Biochem. Biophys. Res. Comm. 83, 1132–1139.
Evolutionary change of the heme c electronic structure: ferricytochrome c-551 from Pseudomonas aeruginosa and horse heart ferricytochrome c.

109. Wagner, G., Wüthrich, K. and Tschesche, H. (1978) Eur. J. Biochem. 89, 367–377.
A ¹H nuclear magnetic resonance study of the solution conformation of the isoinhibitor K from Helix pomatia.

110. Wagner, G. and Wüthrich, K. (1978) Nature 275, 247–248.
Dynamic model of globular protein conformations based on NMR studies in solution.

111. Lauterwein, J. and Wüthrich, K. (1978) FEBS Lett. 93, 181–184.
A possible structural basis for the different modes of action of neurotoxins and cardiotoxins from snake venoms.

112. Wüthrich, K. and Wagner, G. (1978) Trends Biochem. Sci. 3, 227–230.
Internal motion in globular proteins.

113. Richarz, R. and Wüthrich, K. (1978) Biopolymers 17, 2133–2141.
Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H–Gly–Gly–X–L-Ala–OH.

114. Wüthrich, K., Wagner, G. and Bundi, A. (1978) in Nuclear Magnetic Resonance Spectroscopy in Molecular Biology (B. Pullman, ed.) pp. 201–210, Reidel, Dordrecht.
NMR studies of the molecular dynamics of peptides and proteins.

115. Bundi, A., Andreatta, R.H. and Wüthrich, K. (1978) Eur. J. Biochem. 91, 201–208.
Characterisation of a local structure in the synthetic parathyroid hormone fragment 1–34 by ¹H nuclear magnetic resonance techniques.

116. Bösch, C., Bundi, A., Oppliger, M. and Wüthrich, K. (1978) Eur. J. Biochem. 91, 209–214.
¹H nuclear magnetic resonance studies of the molecular conformation of monomeric glucagon in aqueous solution.

117. Perkins, S.J. and Wüthrich, K. (1978) Biochim. Biophys. Acta 536, 406–420.
Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by ¹H NMR at 360 MHz.

118. Gordon, S.L. and Wüthrich, K. (1978) J. Am. Chem. Soc. 100, 7094–7096.
Transient proton–proton Overhauser effects in horse ferrocytochrome c.

119. DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 2727–2742.
¹H–¹⁵N spin–spin couplings in alumichrome.

120. Lauterwein, J., Lazdunski, M. and Wüthrich, K. (1978) Eur. J. Biochem. 92, 361–71.
The ¹H nuclear magnetic resonance spectra of neurotoxin I and cardiotoxin V^II4 from Naja mossambica mossambica.

121. Llinás, M., Klein, M.P. and Wüthrich, K. (1978) Biophys. J. 24, 849–862.
Amide proton spin–lattice relaxation in polypeptides: a field-dependence study of the proton and nitrogen dipolar interactions in alumichrome.

122. Viti, V., Wüthrich, K., Giacometti, G. and Brunori, M. (1978) in Proceedings of the European Conference on NMR of Macromolecules (F. Conti, ed.) pp. 509–516, Lerici, Sassari, Italy.
¹H NMR studies of structural aspects of the root effect in trout hemoglobin.

123. Nagayama, K., Bachmann, P., Ernst, R.R. and Wüthrich, K. (1979) Biochem. Biophys. Res. Comm. 86, 218–225.
Selective spin decoupling in the J-resolved two-dimensional ¹H NMR spectra of proteins.

124. Perkins, S.J. and Wüthrich, K. (1979) Biochim. Biophys. Acta 576, 409–423.
Ring current effects in the conformation-dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor.

125. Bundi, A. and Wüthrich, K. (1979) Biopolymers 18, 285–297.
¹H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H–Gly–Gly–X–L-Ala–OH.

126. Bundi, A. and Wüthrich, K. (1979) Biopolymers 18, 299–311.
Use of amide ¹H NMR titration shifts for studies of polypeptide conformation.

127. Wüthrich, K., Wagner, G. and Richarz, R. (1979) in Protein: Structure, Function and Industrial Applications (E. Hofmann, W. Pfeil and H. Aurich, eds.) pp. 143–152, Pergamon, New York.
A dynamic model for globular protein conformations based on high resolution NMR data.

128. Wüthrich, K., Keller, R.M. and Gordon, S.L. (1978) in Frontiers of Biological Energetics, (P.L.Dutton, J. Leigh and A. Scarpa, eds.) Vol. I, pp. 109–117, Academic Press, New York.
Evolutionary changes of the heme c electronic structure in cytochromes c.

129. Dubs, A., Wagner, G. and Wüthrich, K. (1979) Biochim. Biophys. Acta 577, 177–194.
Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor.

130. Wagner, G., Tschesche, H. and Wüthrich, K. (1979) Eur. J. Biochem. 95, 239–248.
The influence of localized chemical modifications of the basic pancreatic trypsin inhibitor on static and dynamic aspects of the molecular conformation in solution.

131. Wagner, G., Kalb (Gilboa), A.J. and Wüthrich, K. (1979) Eur. J. Biochem. 95, 249–253.
Conformational studies by ¹H nuclear magnetic resonance of the basic pancreatic trypsin inhibitor after reduction of the disulfide bond between Cys-14 and Cys-38.

132. Wagner , G. and Wüthrich, K. (1979) J. Magn. Reson. 33, 675–680.
Truncated driven nuclear Overhauser effect (TOE): a new technique for studies of selective ¹H–¹H Overhauser effects in the presence of spin diffusion.

133. Wüthrich, K. and Wagner, G. (1979) J. Mol. Biol. 130, 1–18.
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.

134. Richarz, R., Sehr, P., Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 130, 19–30.
Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor.

135. Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 130, 31–37.
Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.

136. Wüthrich, K., Nagayama, K. and Ernst, R.R. (1979) Trends Biochem. Sci. 4, N178–N181.
Two-dimensional NMR spectroscopy.

137. Nagayama, K., Wüthrich, K. and Ernst, R.R. (1979) Biochem. Biophys. Res. Comm. 90, 305–311.
Two-dimensional spin echo correlated spectroscopy (SECSY) for ¹H NMR studies of biological macromolecules.

138. Lauterwein, J., Bösch, C., Brown, L.R. and Wüthrich, K. (1979) Biochim. Biophys. Acta 556, 244–264.
Physicochemical studies of the protein–lipid interactions in melittin-containing micelles.

139. Keller, R.M., Picot, D. and Wüthrich, K. (1979) Biochim. Biophys. Acta 580, 259–265.
Individual assignments of the heme resonances in the 360 MHz ¹H NMR spectra of cytochrome c-557 from Crithidia oncopelti.

140. Hetzel, R. and Wüthrich, K. (1979) Biopolymers 18, 2589–2606.
Conformational energy studies of linear dipeptides H-X-L-Pro-OH.

141. Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 134, 75–94.
Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins.

142. Ernst, R.R., Aue, W.P., Bachmann, P., Höhener, A., Linder, M., Meier, B., Müller, L., Wokaun, A., Nagayama, K., Wüthrich, K. and Jeener, J. (1978) Proc. XXth Congress AMPERE, Tallinn, 15–18.
Applications of two-dimensional spectroscopy to problems of physical, chemical and biological relevance.

143. Vašák, M., Nagayama, K., Wüthrich, K., Mertens, M.L. and Kägi, J.H.R. (1979) Biochemistry 18, 5050–5055.
Creatine kinase: nuclear magnetic resonance and fluorescence evidence for interactions of adenosine 5’-diphosphate with aromatic residues.

144. Richarz, R., Tschesche, H. and Wüthrich, K. (1979) Eur. J. Biochem. 102, 563–571.
Structural characterization by nuclear magnetic resonance of a reactive-site carbon-13-labelled basic pancreatic trypsin inhibitor with the peptide bond Arg-39 – Ala-40 cleaved and Arg-39 removed.

145. Wüthrich, K. (1979) Japanese Edition of 'NMR in Biological Research: Peptides and Proteins' (Translation by Y. Arata and M. Kainosho). Kagaku Dozin, Tokyo, Japan.

146. Keller, R.M. and Wüthrich, K. (1980) Biochim. Biophys. Acta 621, 204–217.
Structural study of the heme crevice in cytochrome b₅ based on individual assignments of the ¹H NMR lines of the heme group and selected amino acid residues.

147. Wüthrich, K., Roder, H. and Wagner, G. (1980) in Protein Folding (R. Jaenicke, ed.) pp. 549–564, North-Holland, Amsterdam.
Internal mobility and unfolding of globular proteins.

148. Senn, H., Keller, R.M. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 92, 1362–1369.
Different chirality of the axial methionine in homologous cytochromes c determined by ¹H NMR and CD spectroscopy.

149. Wüthrich, K. (1980) in Frontiers of Bioorganic Chemistry and Molecular Biology (S.N.Ananchenko, ed.) pp. 161–168, Pergamon Press, Oxford.
Complementation of protein crystal structures by NMR studies in solution.

150. Lauterwein, J., Brown, L.R. and Wüthrich, K. (1980) Biochim. Biophys. Acta 622, 219–230.
High-resolution ¹H NMR studies of monomeric melittin in aqueous solution.

151. Brown, L.R., Lauterwein, J. and Wüthrich, K. (1980) Biochim. Biophys. Acta 622, 231–244.
High-resolution ¹H NMR studies of self-aggregation of melittin in aqueous solution.

152. Perkins, S.J. and Wüthrich, K. (1980) J. Mol. Biol. 138, 43–64.
Conformational transition from trypsinogen to trypsin: ¹H nuclear magnetic resonance at 360 MHz and ring current calculations.

153. Anil-Kumar, Ernst, R.R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 95, 1–6.
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton–proton cross-relaxation networks in biological macromolecules.

154. Wüthrich, K., Bösch, C. and Brown, L.R. (1980) Biochem. Biophys. Res. Comm. 95, 1504–1509.
Conformational studies of lipid-bound polypeptides by elucidation of proton–proton cross-relaxation networks.

155. Nagayama, K., Anil-Kumar, Wüthrich, K. and Ernst, R.R. (1980) J. Magn. Reson. 40, 321–334.
Experimental techniques of two-dimensional correlated spectroscopy.

156. Anil-Kumar, Wagner, G., Ernst, R.R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 96, 1156–1163.
Studies of J-connectivities and selective ¹H–¹H Overhauser effects in H₂O solutions of biological macromolecules by two-dimensional NMR experiments.

157. Wüthrich, K., Wagner, G., Richarz, R. and Braun, W. (1980) Biophys. J. 32, 549–560.
Correlations between internal mobility and stability of globular proteins.

158. Keller, R.M., Schejter, A. and Wüthrich, K. (1980) Biochim. Biophys. Acta 626, 15–22.
¹H NMR studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c-552 from Euglena gracilis.

159. Grathwohl, C. and Wüthrich, K. (1981) in Perspectives in Peptide Chemistry (A. Eberle, R. Geiger and T. Wieland, eds.) pp. 249–260, Karger, Basel.
Nuclear magnetic resonance studies of peptide and protein conformations.

160. Richarz, R., Nagayama, K. and Wüthrich, K. (1980) Biochemistry 19, 5189–5196.
Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogue.

161. Richarz, R., Tschesche, H. and Wüthrich, K. (1980) Biochemistry 19, 5711–5715.
Carbon-13 nuclear magnetic resonance studies of the selectively isotope-labeled reactive site peptide bond of the basic pancreatic trypsin inhibitor in the complexes with trypsin, trypsinogen and anhydrotrypsin.

162. Wüthrich, K., Eugster, A. and Wagner, G. (1980) J. Mol. Biol. 144, 601–604.
p²H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 14–38.

163. Bösch, C., Brown, L.R. and Wüthrich, K. (1980) Biochim. Biophys. Acta 603, 298–312.
Physicochemical characterization of glucagon-containing lipid micelles.

164. Wüthrich, K. and Wagner, G. (1980) in Biomolecular Structure, Conformation, Function and Evolution, Vol. 2: Physico-Chemical and Theoretical Studies (R. Srinivasan, ed.) pp. 23-29, Pergamon Press, Oxford.
Dynamic aspects of protein conformation studied by nuclear magnetic resonance techniques: evidence for hydrophobic stability domains in globular proteins.

165. Nagayama, K. and Wüthrich, K. (1981) Eur. J. Biochem. 114, 365–374.
Systematic application of two-dimensional ¹H nuclear magnetic resonance techniques for studies of proteins 1: combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino acid residues.

166. Wagner, G., Anil-Kumar and Wüthrich, K. (1981) Eur. J. Biochem. 114, 375–384.
Systematic application of two-dimensional ¹H nuclear magnetic resonance techniques for studies of proteins 2: combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidation of polypeptide secondary structures.

167. Braun, W., Bösch, C., Brown, L.R., Gō , N. and Wüthrich, K. (1981) Biochim. Biophys. Acta 667, 377–396.
Combined use of proton–proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations: application to micelle-bound glucagon.

168. Bösch, C., Anil-Kumar, Baumann, R., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 42, 159–163.
Comparison of selective proton–proton Overhauser effects in biological macromolecules observed by one-dimensional and two-dimensional NMR experiments.

169. Wider, G., Baumann, R., Nagayama, K., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 42, 73–87.
Strong spin–spin coupling in the two-dimensional J-resolved 360 MHz ¹H NMR spectra of the common amino acids.

170. Brown, L.R., Bösch, C. and Wüthrich, K. (1981) Biochim. Biophys. Acta 642, 296–312.
Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies.

171. Nagayama, K. and Wüthrich, K. (1981) Eur. J. Biochem. 115, 653–657.
Structural interpretation of vincinal proton–proton coupling constants ³J_ab in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy.

172. Keller, R.M. and Wüthrich, K. (1981) Biochim. Biophys. Acta 668, 307–320.
¹H NMR studies of structural homologies between the heme environments in horse cytochrome c and in cytochrome c-552 from Euglena gracilis.

173. Wüthrich, K. (1981) in Lectures Delivered at the International Winter School on Current Trends in Biomolecular Structures (R. Srinivasan, ed.) pp. 271–293, Macmillan India, Madras.
High resolution nuclear magnetic resonance (NMR) studies of peptides and proteins.

174. Anil-Kumar, Wagner, G., Ernst, R.R. and Wüthrich, K. (1981) J. Am. Chem. Soc. 103, 3654–3658.
Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation.

175. Possani, L., Steinmetz, W.E., Dent, M.A.R., Alagón, A.C. and Wüthrich, K. (1981) Biochim. Biophys. Acta 669, 183–192.
Preliminary spectroscopic characterization of six toxins from latin american scorpions.

176. Baumann, R., Anil-Kumar, Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 44, 76–83.
Improvement of 2D NOE and 2D correlated spectra by triangular multiplication.

177. Keller, R.M. and Wüthrich, K. (1981) in Biological Magnetic Resonance (L.J. Berliner and J.Reuben, eds.) Vol. 3, 1–52, Plenum Press, New York.
Multiple irradiation ¹H NMR experiments with hemoproteins.

178. Nagayama, K. and Wüthrich, K. (1980) in Protein Dynamics and Energy Transduction, pp. 83–12, Taniguchi Foundation, Osaka.
An application of two-dimensional NMR techniques for studies of the rotational mobility of the amino acid side chains about the C^a–C^b bonds in basic pancreatic trypsin inhibitor.

179. Wüthrich, K., Richarz, R., Perkins, S.J. and Tschesche, H. (1981) in Structural Aspects of Recognition and Assembly in Biological Macromolecules (M. Balaban, J.L. Sussman, W. Traub and A. Yonath, eds.) pp. 21–34, Balaban ISS, Rehovot.
Protein–protein interactions in the complexes formed between the basic pancreatic trypsin inhibitor (BPTI) and trypsin or trypsinogen: studies in solution by ¹³C NMR and ¹H NMR.

180. Baumann, R., Wider, G., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 44, 402–406.
Improvement of 2D NOE and 2D correlated spectra by symmetrization.

181. Brown, L.R. and Wüthrich, K. (1981) Biochim. Biophys. Acta 647, 95–111.
Melittin bound to dodecylphosphocholine micelles: ¹H NMR assignments and global conformational features.

182. Wüthrich, K. (1981) Biochem. Soc. Symp. 46, 17–37.
Nuclear magnetic resonance studies of internal mobility in globular proteins.

183. Grathwohl, C. and Wüthrich, K. (1981) Biopolymers 20, 2623–2633.
NMR studies of the rates of proline cis-trans isomerization in oligopeptides.

184. Steinmetz, W.E., Moonen, X., Anil-Kumar, Lazdunski, M., Visser, L., Carlsson, F.H.H. and Wüthrich, K. (1981) Eur. J. Biochem. 120, 467–475.
¹H nuclear magnetic resonance studies of the conformation of cardiotoxin V^II2 from Naja mossambica mossambica.

185. Brown, L.R., Braun, W., Anil-Kumar and Wüthrich, K. (1982) Biophys. J. 37, 319–328.
High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid–water interface.

186. Macura, S., Wüthrich, K. and Ernst, R.R. (1982) J. Magn. Reson. 46, 269–282.
Separation and suppression of coherent transfer effects in two-dimensional NOE and chemical exchange spectroscopy.

187. Wüthrich, K., Wider, G., Wagner, G. and Braun, W. (1982) J. Mol. Biol. 155, 311–319.
Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance.

188. Billeter, M., Braun, W. and Wüthrich, K. (1982) J. Mol. Biol. 155, 321–346.
Sequential resonance assignments in protein ¹H nuclear magnetic resonance spectra: computation of sterically allowed proton–proton distances and statistical analysis of proton– proton distances in single crystal protein conformations.

189. Wagner, G. and Wüthrich, K. (1982) J. Mol. Biol. 155, 347–366.
Sequential resonance assignments in protein ¹H nuclear magnetic resonance spectra: basic pancreatic trypsin inhibitor.

190. Wider, G., Lee, K.H. and Wüthrich, K. (1982) J. Mol. Biol. 155, 367–388.
Sequential resonance assignments in protein ¹H nuclear magnetic resonance spectra: glucagon bound to perdeuterated dodecylphosphocholine micelles.

191. Macura, S., Wüthrich, K. and Ernst, R.R. (1982) J. Magn. Reson. 47, 351–357.
The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules.

192. Wüthrich, K. (1982) in Structural Molecular Biology (D.B. Davies, W. Saenger and S.S. Danyluk, eds.) pp. 215–235 Plenum Press, New York.
High resolution NMR experiments for studies of protein conformations.

193. Arseniev, A.S., Wider, G., Joubert, F.J. and Wüthrich, K. (1982) J. Mol. Biol. 159, 323–351.
Assignment of the ¹H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis: two-dimensional nuclear magnetic resonance at 500 MHz.

194. Wagner, G. and Wüthrich, K. (1982) J. Mol. Biol. 160, 343–361.
Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution: studies with two-dimensional nuclear magnetic resonance.

195. Wüthrich, K. (1982) Die Umschau 82, 684–690.
Die Struktur von nicht-kristallinen Proteinen.

196. Keller, R.M., Baumann, R., Hunziker-Kwik, E.H., Joubert , F.J. and Wüthrich, K. (1983) J. Mol. Biol. 163, 623–646.
Assignment of the ¹H nuclear magnetic resonance spectrum of the trypsin inhibitor homologue K from Dendroaspis polylepis polylepis: two-dimensional nuclear magnetic resonance at 360 and 500 MHz.

197. Wüthrich, K., Bösch, C., Braun, W., Brown, L.R., Lee, K.H. and Wider, G. (1982) in Structure of Complexes between Biopolymers and Low Molecular Weight Molecules, (W. Bartmann and G. Snatzke, eds.) pp. 45–155, Wiley, New York.
NMR studies of the conformation of polypeptide chains bound to lipid micelles.

198. Wüthrich, K. and Wagner, G. (1983) in Mobility and Function in Proteins and Nucleic Acids (R.Porter, M. O’Connor and J. Whelan, eds.) pp. 310–328, Pitman, London.
Nuclear magnetic resonance studies of mobility in proteins.

199. Hosur, R.V., Wider, G. and Wüthrich, K. (1983) Eur. J. Biochem. 130, 497–508.
Sequential individual resonance assignments in the ¹H nuclear magnetic resonance spectrum of cardiotoxin V^II2 from Naja mossambica mossambica.

200. Senn, H., Eugster, A. and Wüthrich, K. (1983) Biochim. Biophys. Acta 743, 58–68.
Determination of the coordination geometry at the heme iron in three cytochromes c from Saccharomyces cerevisiae and from Cadida krusei based on individual ¹H NMR assignments for heme c and the axially coordinated amino acids.

201. Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 743, 69–81.
Individual ¹H NMR assignments for the heme groups and the axially bound amino acids and determination of the coordination geometry at the heme iron in a mixture of two isocytochromes c‑551 from Rhodopseudomonas gelatinosa.

202. Wagner, G. und Wüthrich, K. (1983) Naturwissenschaften 70, 105–114.
Dynamik von Protein-Strukturen.

203. Wüthrich, K. (1983) Biopolymers 22, 131–138.
Sequential individual resonance assignments in the ¹H-NMR spectra of polypeptides and proteins.

204. Wider, G., Hosur, R.V. and Wüthrich, K. (1983) J. Magn. Reson. 52, 13–135.
Suppression of the solvent resonance in 2D NMR spectra of proteins in H₂O solution.

205. Wüthrich, K. (1983) in Fortschrittsberichte aus Naturwissenschaft und Medizin (H.A. Staab, W.Gerok, H. Markl, W. Martienssen und H. Gibian, eds.) pp. 169–182, Wissenschaftliche Verlagsgesellschaft, Stuttgart.
Räumliche Struktur von Proteinen in Lösung und in Lipid–Wasser-Grenzschichten.

206. Pardi, A., Walker, R., Rapoport, H., Wider, G. and Wüthrich, K. (1983) J. Am. Chem. Soc. 105, 1652–1653.
Sequential assignments for the ¹H and ³¹P atoms in the backbone of oligonucleotides by two-dimensional nuclear magnetic resonance.

207. Strop , P. and Wüthrich, K. (1983) J. Mol. Biol. 166, 631–640.
Characterization of the proteinase inhibitor IIA from bull seminal plasma by ¹H nuclear magnetic resonance: stability, amide proton exchange and mobility of aromatic residues.

208. Strop , P., Wider, G. and Wüthrich, K. (1983) J. Mol. Biol. 166, 641–667.
Assignment of the ¹H nuclear magnetic resonance spectrum of the proteinase inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic resonance at 500 MHz.

209. Strop , P., ÚCechová , D. and Wüthrich, K. (1983) J. Mol. Biol. 166, 669–676.
Preliminary structural comparison of the proteinase isoinhibitors IIA and IIB from bull seminal plasma based on individual assignments of the ¹H nuclear magnetic resonance spectra by two-dimensional nuclear magnetic resonance at 500 MHz.

210. Marion, D. and Wüthrich, K. (1983) Biochem. Biophys. Res. Comm. 113, 967–974.
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of ¹H–¹H spin–spin coupling constants in proteins.

211. Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 746, 48–60.
Conformation of the axially bound ligands of the heme iron and electronic structure of heme c in the cytochromes c-551 from Pseudomonas mendocina and Pseudomonas stutzeri and in cytochrome c from Rhodospirillum rubrum.

212. Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 747, 16–25.
A new spatial structure for the axial methionine observed in cytochrome c₅ from Pseudomonas mendocina: correlations with the electronic structure of heme c.

213. Hosur, R.V., Ernst, R.R. and Wüthrich, K. (1983) J. Magn. Reson. 54, 142–145.
A simple two-dimensional measurement of the decoupler power during continuous homonuclear irradiation for the correction of Bloch-Siegert shifts.

214. Wagner, G., Pardi, A. and Wüthrich, K. (1983) J. Am. Chem. Soc. 105, 5948–5949.
Hydrogen bond length and ¹H NMR chemical shifts in proteins.

215. Braun, W., Wider, G., Lee, K.H. and Wüthrich, K. (1983) J. Mol. Biol. 169, 921–948.
Conformation of glucagon in a lipid–water interphase by ¹H nuclear magnetic resonance.

216. Wüthrich, K., Billeter, M. and Braun, W. (1983) J. Mol. Biol. 169, 949–961.
Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton–proton distance constraints with nuclear magnetic resonance.

217. Zuiderweg, E.R.P., Kaptein, R. and Wüthrich, K. (1983) Proc. Natl. Acad. Sci. USA 80, 5837–5841.
Secondary structure of the lac repressor DNA-binding domain by two-dimensional ¹H nuclear magnetic resonance in solution.

218. Senn, H., Guerlesquin, F., Bruschi, M. and Wüthrich, K. (1983) Biochim. Biophys. Acta 748, 194–204.
Coordination of the heme iron in the low-potential cytochrome c-553 from Desulfovibrio vulgaris and Desulfovibrio desulfuricans. Different chirality of the axially bound methionine in the oxidized and reduced states.

219. Zuiderweg, E.R.P., Kaptein, R. and Wüthrich, K. (1983) Eur. J. Biochem. 137, 279–292.
Sequence-specific resonance assignments in the ¹H nuclear magnetic resonance spectrum of the lac repressor DNA-Binding domain 1–51 from Escherichia coli by two-dimensional spectroscopy.

220. Pardi, A., Wagner, G. and Wüthrich, K. (1983) Eur. J. Biochem. 137, 445–454.
Protein conformation and proton nuclear magnetic resonance chemical shifts.

221. Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R. and Wüthrich, K. (1983) Biochem. Biophys. Res. Comm. 117, 479–485.
Improved spectral resolution in COSY ¹H NMR spectra of proteins via double quantum filtering.

222. Wider, G., Macura, S., Anil Kumar, Ernst, R.R. and Wüthrich, K. (1984) J. Magn. Reson. 56, 207–234.
Homonuclear two-dimensional ¹H NMR of proteins: experimental procedures.

223. Senn, H., Cusanovich, M.A. and Wüthrich, K. (1984) Biochim. Biophys. Acta 785, 46–53.
¹H NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555.

224. Williamson, M.P., Marion, D. and Wüthrich, K. (1984) J. Mol. Biol. 173, 341–359.
Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance.

225. Neuhaus, D., Wider, G., Wagner, G. and Wüthrich, K. (1984) J. Magn. Reson. 57, 164–168.
X-relayed ¹H–¹H correlated spectroscopy.

226. Wüthrich, K. and Wagner, G. (1984) Trends Biochem. Sci. 9, 152–154.
Internal dynamics of proteins.

227. Senn, H., Billeter, M. and Wüthrich, K. (1984) Eur. Biophys. J. 11, 3–15.
The spatial structure of the axially bound methionine in solution conformations of horse ferrocytochrome c and Pseudomonas aeruginosa ferrocytochrome c 551 by ¹H NMR.

228. Wüthrich, K., ÚStrop,, P., Ebina, S. and Williamson, M.P. (1984) Biochem. Biophys. Res. Comm. 122, 1174–1178.
A globular protein with slower amide proton exchange from an a helix than from antiparallel b sheets.

229. Rance, M., Wagner, G., Sørensen, O.W., Wüthrich, K. and Ernst, R.R. (1984) J. Magn. Reson. 59, 250–261.
Applications of w₁-decoupled 2D correlation spectra to the study of proteins.

230. Senn, H., Böhme, H. and Wüthrich, K. (1984) Biochim. Biophys. Acta 789, 311–323.
Studies of the solution conformation of Spirulina platensis cytochrome c-553 by ¹H nuclear magnetic resonance and circular dichroism.

231. Neuhaus, D., Wagner, G., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1984) Eur. J. Biochem. 143, 659–667.
¹¹³Cd–¹H spin–spin couplings in homonuclear ¹H correlated spectroscopy of metallothionein: identification of the cysteine ¹H spin systems.

232. Zuiderweg, E.R.P., Billeter, M., Boelens, R., Scheek, R.M., Wüthrich, K. and Kaptein, R. (1984) FEBS Lett. 174, 243–247.
Spatial arrangement of the three a helices in the solution conformation of E. coli lac repressor DNA-binding domain.

233. Havel, T.F. and Wüthrich, K. (1984) Bull. Math. Biol. 46, 673–698.
A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular ¹H–¹H proximities in solution.

234. Stassinopoulou, C.I., Wagner, G. and Wüthrich, K. (1984) Eur. J. Biochem. 145, 423–430.
Two-dimensional ¹H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor: sequence specific resonance assignments and sequence location of conformation changes relative to the native protein.

235. Wagner, G., Stassinopoulou, C.I. and Wüthrich, K. (1984) Eur. J. Biochem. 145, 431–436.
Amide proton exchange studies by two-dimensional correlated ¹H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor.

236. Ebina, E. and Wüthrich, K. (1984) J. Mol. Biol. 179, 283–288.
Amide proton titration shifts in bull seminal inhibitor IIA by two-dimensional correlated ¹H nuclear magnetic resonance (COSY): manifestation of conformational equilibria involving carboxylate groups.

237. Bodenhausen, G., Wagner, G., Rance, M., Sørensen, O.W., Wüthrich , K. and Ernst, R.R. (1984) J.Magn. Reson. 59, 542–550.
Longitudinal two-spin order in 2D exchange spectroscopy (NOESY).

238. Zuiderweg, E.R.P., Billeter, M. Kaptein, R., Boelens, R., Scheek , R.M. and Wüthrich, K. (1984) in Progress in Bioorganic Chemistry and Molecular Biology (Yu.A. Ovchinnikov, ed.) pp. 65–70, Elsevier, Amsterdam.
Solution conformation of E. coli lac repressor DNA-binding domain by 2D NMR: sequence location and spatial arrangement of three a-helices.

239. Wüthrich, K. (1981) Makromol. Chem. Suppl. 5, 234–252.
Studies of static and dynamic aspects of spatial protein structures by high resolution nuclear magnetic resonance spectroscopy.

240. Wüthrich, K., Billeter, M. and Braun, W. (1984) J. Mol. Biol. 180, 715–740.
Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton–proton distances.

241. Pardi, A., Billeter, M. and Wüthrich, K. (1984) J. Mol. Biol. 180, 741–751.
Calibration of the angular dependence of the amide proton–C^a proton coupling constants, ³J_HNa , in a globular protein: use of ³J_HNa for identification of helical secondary structure.

242. Rance, M., Sørensen, O.W., Leupin, W., Kogler, H., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 61, 67–80.
Uniform exitation of multiple quantum coherence: application to two-dimensional double- quantum spectroscopy.

243. Wüthrich, K. (1984) Biomed. Res. 5, 151–160.
Three-dimensional structure of non crystalline polypeptides by nuclear magnetic resonance.

244. Havel, T.F. and Wüthrich, K. (1985) J. Mol. Biol. 182, 281–294.
An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution.

245. Williamson, M.P., Havel, T.F. and Wüthrich, K. (1985) J. Mol. Biol. 182, 295–315.
Solution conformation of proteinase inhibitor IIA from bull seminal plasma by ¹H nuclear magnetic resonance and distance geometry.

246. Kline, A.D. and Wüthrich, K. (1985) J. Mol. Biol. 183, 503–507.
Secondary structure of the a-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by ¹H nuclear magnetic resonance.

247. Denk, W., Wagner, G., Rance, M. and Wüthrich, K. (1985) J. Magn. Reson. 62, 350–355.
Combined suppression of diagonal peaks and t₁-ridges in two-dimensional nuclear Overhauser enhancement spectra.

248. Billeter, M., Engeli, M. and Wüthrich, K. (1985) J. Mol. Graphics 3, 79–83, 97–98.
Interactive program for investigation of protein structures based on ¹H NMR experiments.

249. Roder, H., Wagner, G. and Wüthrich, K. (1985) Biochemistry 24, 7396–7407.
Amide proton exchange in proteins by EX₁ kinetics: studies of the basic pancreatic trypsin inhibitor at variable p²H and temperature.

250. Roder, H., Wagner, G. and Wüthrich, K. (1985) Biochemistry 24, 7407–7411.
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor.

251. Rance, M., Bodenhausen, G., Wagner, G., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 62, 497–510.
A systematic approach to the suppression of J cross peaks in 2D exchange and 2D NOE spectroscopy.

252. Guerlesquin, F., Bruschi, M. and Wüthrich, K. (1985) Biochim. Biophys. Acta 830, 296–303.
¹H NMR studies of Desulfovibrio desulfuricans Norway strain cytochrome c₃.

253. Müller, N., Bodenhausen, G., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 65, 531–534.
The appearance of forbidden cross peaks in two-dimensional nuclear magnetic resonance spectra due to multiexponential T₂ relaxation.

254. Frey, M.H., Leupin, W., Sørensen, O.W., Denny, W.A., Ernst, R.R. and Wüthrich, K. (1985) Biopolymers 24, 2371–2380.
Sequence-specific assignment of the backbone ¹H- and ³¹P-NMR lines in a short DNA duplex with homo- and heteronuclear correlated spectroscopy.

255. Chazin, W.J., Goldenberg, D.P., Creighton, T.E. and Wüthrich, K. (1985) Eur. J. Biochem. 152, 429–437.
Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by ¹H nuclear magnetic resonance in solution.

256. Wagner, G. , Bodenhausen, G., Müller, N., Rance, M., Sørensen, O.W., Ernst, R.R. and Wüthrich, K. (1985) J. Am. Chem. Soc. 107, 6440–6446.
Exchange of two-spin order in nuclear magnetic resonance: separation of exchange and cross relaxation processes.

257. Frey, M.H., Wagner, G., Vašák, M., Sørensen, O.W., Neuhaus, D., Wörgötter, E., Kägi, J.H.R., Ernst, R.R. and Wüthrich, K. (1985) J. Amer. Chem. Soc. 107, 6847–6851.
Polypeptide metal cluster connectivities in metallothionein-2 by novel ¹H–¹¹³Cd heteronuclear two-dimensional NMR experiments.

258. Neuhaus, D., Wagner, G., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1985) Eur. J. Biochem. 151, 257–273.
Systematic application of high resolution, phase-sensitive two- dimensional ¹H NMR techniques for the identification of the amino acid proton spin systems in proteins: rabbit metallothionein-2.

259. Wüthrich, K. (1986) Europhysics News 17, 11–13.
NMR with proteins and nucleic acids.

260. Braun, W., Wagner, G., Wörgötter, E., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1986) J. Mol. Biol. 187, 125–129.
Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution.

261. Wagner, G., Neuhaus, D., Wörgötter, E., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1986) J Mol. Biol. 187, 131–135.
Nuclear magnetic resonance identification of “half-turn” and 3₁₀ -helix secondary structure in rabbit liver metallothionein-2.

262. Senn, H. and Wüthrich, K. (1985) Q. Rev. Biophys. 18, 111–134.
Amino acid sequence, haem iron coordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes.

263. Otting, G., Widmer, H., Wagner, G. and Wüthrich, K. (1986) J. Magn. Reson. 66, 187–193.
Origin of t₁ and t₂ ridges in 2D NMR spectra and procedures for suppression.

264. Otting, G. and Wüthrich, K. (1986) J. Magn. Reson. 66, 359–363.
Complete protein fingerprints by double quantum spectroscopy.

265. Wagner, G., Neuhaus, D., Wörgötter, E., Vašák, M., Kägi , J.H.R. and Wüthrich, K. (1986) Eur.J. Biochem. 157, 275–289.
Sequence-specific ¹H NMR assignments in rabbit liver metallothionein-2.

266. Schultze, P. and Wüthrich, K. (1986) J. Mol. Graphics 4, 105–111.
Display algorithm for space filling molecular models using a video array processor.

267. Kline, A.D., Braun, W. and Wüthrich, K. (1986) J. Mol. Biol. 189, 377–382.
Studies by ¹H nuclear magnetic resonance and distance geometry of the solution conformation of the a-amylase inhibitor Tendamistat.

268. Wagner, G. and Wüthrich, K. (1986) Eur. J. Biochem. 157, 618.
Reply to the comments by C.E. Dempsey on “Amide proton exchange studies by two-dimensional correlated ¹H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor”, by G. Wagner, C.I. Stassinopoulou and K. Wüthrich.

269. Wüthrich, K. (1986) in NMR in the Life Sciences (E.M. Bradbury and C. Nicolini, eds.) NATO ASI Series A: Life Sciences 107, 11–22, Plenum Press, New York.
2D NMR with biopolymers.

270. Wüthrich, K. (1986) in Design and Synthesis of Organic Molecules Based on Molecular Recognition, Proc. XVIIth Solvay Conference on Chemistry (G. van Binst, ed.) pp. 52–56, Springer, Berlin.
Glucagon conformation in different environments: implications for molecular recognition.

271. Chazin, W.J., Wüthrich, K., Hyberts, S., Rance, M., Denny, W.A. and Leupin, W. (1986) J. Mol. Biol. 190, 439–453.
¹H nuclear magnetic resonance assignments for d-(GCATTAATGC)₂ using experimental refinements of established procedures.

272. Roder, H. and Wüthrich, K. (1986) Proteins 1, 34–42.
Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons.

273. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.

274. Wüthrich, K. (1986) in X National NMR Symposium of Finland (E. Kolehmainen, ed.) pp. 1–23, Publications of the University of Kuopio, Vol. 3, Kuopio.
Nuclear magnetic resonance with proteins and nucleic acids.

275. Wörgötter, E., Wagner, G. and Wüthrich, K. (1986) J. Am. Chem. Soc. 108, 6162– 6167.
Simplification of two-dimensional ¹H NMR spectra using an X-filter.

276. Müller, N., Ernst, R.R. and Wüthrich, K. (1986) J. Am. Chem. Soc. 108, 6482–6492.
Multiple-quantum-filtered two-dimensional correlated NMR spectroscopy of proteins.

277. Leupin, W., Chazin, W.J., Hyberts, S., Denny, W.A. and Wüthrich, K. (1986) Biochemistry 25, 5902–5910.
NMR studies of the complex between the decadeoxynucleotide d-(GCATTAATGC)₂ and a minor-groove-binding drug.

278. Wagner, G. and Wüthrich, K. (1986) in Enzyme Structure, Part L (C.H.W. Hirs and S.N.Timasheff, eds.) Methods in Enzymology 131, 307–326.
Observation of internal motility of proteins by nuclear magnetic resonance in solution.

279. Montelione, G.T., Wüthrich, K., Nice, E.C., Burgess, A.W. and Scheraga, H.A. (1986) Proc. Natl. Acad. Sci. USA 83, 8594–8598.
Identification of two antiparallel b-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.

280. Widmer, H. and Wüthrich, K. (1986) J. Magn. Reson. 70, 270–279.
Simulation of two-dimensional NMR experiments using numerical density matrix calculations.

281. Kline, A.D. and Wüthrich, K. (1986) J. Mol. Biol. 192, 869–890.
Complete sequence-specific ¹H nuclear magnetic resonance assignments for the a-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae.

282. Senn, H., Eugster, A., Otting, G., Suter, F. and Wüthrich, K. (1987) Eur. Biophys. J. 14, 301–306.
¹⁵N-labeled P22 c2 repressor for nuclear magnetic resonance studies of protein–DNA interactions.

283. Otting, G., Senn, H., Wagner, G. and Wüthrich, K. (1986) J.Magn. Reson. 70, 500–505.
Editing of 2D ¹H NMR spectra using X half-filters: combined use with residue-selective ¹⁵N‑labeling of proteins.

284. Senn, H., Otting, G. and Wüthrich, K. (1987) J. Am. Chem. Soc. 109, 1090–1092.
Protein structure and interactions by combined used of sequential NMR assignments and isotope labeling.

285. Leupin, W., Wagner, G., Denny , W.A. and Wüthrich, K. (1987) Nucl. Acids Res. 15, 267–275.
Assignment of the ¹³C nuclear magnetic resonance spectrum of a short DNA-duplex with ¹H detected two-dimensional heteronuclear correlation spectroscopy.

286. Wüthrich, K. (1987) in Structure, Dynamics and Function of Biomolecules (A. Ehrenberg, R.Rigler, A. Gräslund and L. Nilsson, eds.) pp. 104–107, Springer, Berlin.
A NMR view of proteins in solution.

287. Wüthrich, K. (1986) Rev. Magn. Reson. in Medicine 1, 1–20.
Structure and function of proteins and nucleic acids viewed by NMR in solution.

288. Wüthrich, K. (1986) in Structure and Dynamics of Nucleic Acids, Proteins and Membrane, E.Clementi and S. Chin, eds.) pp. 21–29, Plenum Press, New York.
Conformation of non-crystalline proteins viewed by NMR.

289. Billeter, M., Havel, T.F. and Wüthrich, K. (1987) J. Comp. Chem. 8, 132–141.
The ellipsoid algorithm as a method for the determination of polypeptide conformations from experimental distance constraints and energy minimization.

290. Lee, K.H., Fitton, J.E. and Wüthrich, K. (1987) Biochim. Biophys. Acta 911, 144–153.
Nuclear magnetic resonance investigation of the conformation of d- haemolysin bound to dodecylphosphocholine micelles.

291. Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go- , N. and Wüthrich, K. (1987) J. Mol. Biol. 196, 611–639.
Protein structures in solution by nuclear magnetic resonance and distance geometry: the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.

292. Vašák, M., Wörgötter, E., Wagner, G., Kägi, J.H.R. and Wüthrich, K. (1987) J. Mol. Biol. 196, 711–719.
Metal coordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2.

293. Chazin, W.J. and Wüthrich, K. (1987) J. Magn. Reson. 72, 358–363.
Optimization of homonuclear relayed coherence transfer experiments with proteins in H₂O solution.

294. Otting, G., Grütter, R., Leupin, W., Minganti, C., Ganesh, K.N., Sproat, B.S., Gait , M.J. and Wüthrich, K. (1987) Eur. J. Biochem. 166, 215–220.
Sequential NMR assignments of labile protons in DNA using two-dimensional nuclear Overhauser enhancement spectroscopy with three jump-and-return pulse sequences.

295. Widmer, H. and Wüthrich, K. (1987) J. Magn. Reson. 74, 316–336.
Simulated two-dimensional NMR cross peak fine structures for ¹H spin systems in polypeptides and polydeoxynucleotides.

296. Wagner, G., Brühwiler, D. and Wüthrich, K. (1987) J. Mol. Biol. 196, 227–231.
Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance.

297. Widmer, H., Wagner, G. and Wüthrich, K. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.) pp. 498–499 , Schippert, Zürich.
Application of DQF-COSY, RELAYED-COSY and DOUBLE-RELAYED-COSY for the assignment of protein ¹H-NMR spectra.

298. Frey, M.H., Sørensen, O.W., Leupin, W., Denny, W.A., Rance, M., Ernst, R.R. and Wüthrich, K. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.) pp. 500–501, Schippert, Zürich.
Sequential resonance assignments of oligonucleotides with homonuclear and heteronuclear 2D NMR.

299. Bodenhausen, G., Rance, M., Levitt, M.H., Sørensen, O.W., Meier, B.U., Pfändler, P., Denk, W., Wagner, G., Wüthrich, K. and Ernst, R.R. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.) pp. 566–567, Schippert, Zürich.
New approaches to the measurement of cross-relaxation rates by two-dimensional NMR.

300. Otting, G., Marchot, P., Bougis, P.E., Rochat, H. and Wüthrich, K. (1987) Eur. J. Biochem. 168, 603–607.
Monitoring the purification by high-performance liquid chromatography of cardiotoxins from Naja mossambica mossambica using phase-sensitive two-dimensional nuclear magnetic resonance.

301. Otting, G., Steinmetz, W.E., Bougis, P.E., Rochat, H. and Wüthrich, K. (1987), Eur. J. Biochem. 168, 609–620.
Sequence-specific ¹H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica.

302. Wang Q., Kline, A.D. and Wüthrich, K. (1987) Biochemistry 26, 6488–6493.
Amide proton exchange in the a-amylase polypeptide inhibitor Tendamistat studied by two-dimensional ¹H nuclear magnetic resonance.

303. Wüthrich, K. (1987) Optica Pura Y Aplicada 20, 145–151.
Nuclear magnetic resonance with proteins and nucleic acids.

304. Wüthrich, K. (1987) in DNA–Protein Interactions and Gene Regulation, (E.B. Thompson and J.Papaconstantinou, eds.) pp. 87–94, University Press, Austin.
Nuclear magnetic resonance techniques for studies of protein–DNA interactions.

305. Montelione, G.T., Wüthrich, K., Nice, E.C., Burgess, A.W. and Scheraga, H.A. (1987) Proc. Natl. Acad. Sci. USA 84, 5226–5230.
Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.

306. Wörgötter, E., Wagner, G., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1987) Eur. J. Biochem. 167, 457–466.
Sequence-specific ¹H NMR assignments in rat liver metallothionein-2.

307. Wagner, G., Frey, M.E., Neuhaus, D., Wörgötter, E., Braun, W., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1987) in Metallothionein II, (J.H.R. Kägi and Y. Kojima, eds.) Experientia Suppl. 52, 149–157.
Spatial structure of rabbit liver metallothionein-2 in solution by NMR.

308. Wüthrich, K. (1987) Q. Rev. Biophys. 19, 3–5.
Nuclear magnetic resonance — from molecules to man.

309. Wüthrich, K. (1987) Life Sci. Adv. Biochem. 6, 83–87.
Nuclear magnetic resonance with proteins and nucleic acids.

310 Wörgötter, E., Wagner, G., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Am. Chem. Soc. 110, 2388–2393.
Heteronuclear filters for two-dimensional ¹H NMR: identification of the metal-bound amino acids in metallothionein and observation of small heteronuclear long-range couplings.

311. Steinmetz, W.E., Bougis, P.E., Rochat, H., Redwine, O.D., Braun, W. and Wüthrich, K. (1988) Eur. J. Biochem. 172, 101–116.
¹H nuclear magnetic resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins.

312. Siekmann, J., Wenzel, H.R., Schröder, W., Schutt, H., Truscheit, E., Arens, A., Rauenbusch, E., Chazin, W.J., Wüthrich, K. and Tschesche, H. (1987) Biol. Chem. Hoppe-Seyler 368, 1589–1596.
Pyroglutamyl-aprotinin, a new aprotinin homologue from bovine lungs — isolation, properties, sequence analysis and characterization using ¹H nuclear magnetic resonance in solution.

313. Widmer, H., Wagner, G., Schweitz, H., Lazdunski, M. and Wüthrich, K. (1988) Eur. J. Biochem. 171, 177–192.
The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence-specific ¹H NMR assignments.

314. Otting, G. and Wüthrich, K. (1987) J. Magn. Reson. 75, 546–549.
Pre-TOCSY, a new experiment for obtaining complete 2D ¹H NMR spectra of proteins in H₂O solution.

315. Arseniev, A., Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vašák M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Mol. Biol. 201, 637–657.
Three-dimensional structure of rabbit liver [Cd₇]-metallothionein-2a in aqueous solution determined by nuclear magnetic resonance.

316. Otting, G. and Wüthrich, K. (1988) J. Magn. Reson. 76, 569–574.
Efficient purging scheme for proton-detected heteronuclear two-dimensional NMR.

317. Montelione, G.T., Wüthrich, K. and Scheraga, H.A. (1988) Biochemistry 27, 2235–2243.
Sequence-specific ¹H NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor.

318. Wüthrich, K. (1988) Physikalische Blätter 44, 103–109.
Proteinstrukturermittlung in Lösung mittels kernmagnetischer Resonanzspektroskopie.

319. Celda, B., Widmer, H., Leupin, W., Chazin, W.J., Denny, W.A. and Wüthrich, K. (1989) Biochemistry 28, 1462–1471.
Conformational studies of d-(AAAAATTTTT)₂ using constraints from nuclear Overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional ¹H nuclear magnetic resonance spectra.

320. Kline, A.D., Braun, W. and Wüthrich, K. (1988) J. Mol. Biol. 204, 675–724.
Determination of the complete three-dimensional structure of the a-amylase inhibitor Tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry.

321. Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Mol. Biol. 203, 251–268.
Conformation of [Cd₇]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy.

322. Grütter, R., Otting, G., Wüthrich, K. and Leupin, W. (1988) Eur. Biophys. J. 16, 279–286.
O_R3 operator of bacteriophage l in a 23 base-pair DNA fragment: sequence-specific ¹H NMR assignments for the non-labile protons and comparison with the isolated 17 base-pair operator.

323. Wüthrich, K. (1988) in Water and Ions in Biological Systems, (P. Läuger, L. Packer and V.Vasilescu, eds.) pp. 33–41, Birkhäuser, Basel.
Protein molecules in aqueous solution viewed by nuclear magnetic resonance.

324. Wüthrich, K. (1988) GIT Fachz. Lab. 5, 481–488.
Dreidimensionale Proteinstrukturen in Lösung.

325. Wüthrich, K. (1988) in NMR Spectroscopy in Drug Research, (J.W. Jaroszewski, K. Schaumburg and H. Kofod, eds.) pp. 194–208, Munksgaard, Copenhagen.
Three-dimensional protein structures in solution viewed by NMR.

326. Labhardt, A.M., Hunziker-Kwik, E.H. and Wüthrich, K. (1988) Eur. J. Biochem. 177, 295–305.
Secondary structure determination for a-neurotoxin from Dendroaspis polylepis polylepis based on sequence-specific ¹H-nuclear-magnetic-resonance assignments.

327. Martin, E., Bösch, C., Duc, G., Wüthrich, K., Brunner, P. and Fanconi, A. (1988) Helv. paediat. Acta 43, 53–74.
Magnetresonanz in der pädiatrischen Forschung und Klinik. I. Teil: Was können wir von dieser neuen Methode erwarten?

328. Griesinger, C., Otting, G., Wüthrich, K. and Ernst, R.R. (1988) J. Am. Chem. Soc. 110, 7870–7872.
Clean-TOCSY for ¹H spin system identification in macromolecules.

329. Müller, M., Affolter, M., Leupin, W., Otting, G., Wüthrich, K. and Gehring, W.J. (1988) EMBO J. 7, 4299–4304.
Isolation and sequence-specific DNA binding of the Antennapedia homeodomain.

330. Otting, G., Qian, Y.Q., Müller, M., Affolter, M., Gehring, W.J. and Wüthrich, K. (1988) EMBO J. 7, 4305–4309.
Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix-turn-helix motif.

331. Wüthrich, K. (1988) in Protein Structure and Protein Engineering, 39 Colloquium Mosbach (E.L.Winnacker and R. Huber, eds.) pp. 37– 44, Springer, Heidelberg.
The method of protein structure determination by NMR in solution: initial new insights relating to molecular mobility.EMBO

332. Wüthrich, K. (1989) Science 243, 45–50.
Protein structure determination in solution by nuclear magnetic resonance spectroscopy.

333. Wüthrich, K. (1989) Acc. Chem. Res. 22, 36–44.
The development of nuclear magnetic resonance spectroscopy as a technique for protein structure determination.

334. Otting, G. and Wüthrich, K. (1989) J. Am. Chem. Soc. 111, 1871–1875.
Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules.

335. Billeter, M., Kline, A.D., Braun, W., Huber, R. and Wüthrich, K. (1989) J. Mol. Biol. 206, 677–687.
Comparison of the high-resolution structures of the a-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals.

336. Braun, W., Epp, O., Wüthrich, K. and Huber, R. (1989) J. Mol. Biol. 206, 669–676.
Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial model.

337. Haruyama, H. and Wüthrich, K. (1989) Biochemistry 28, 4301–4312.
Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance.

338. Haruyama, H., Qian, Y.Q. and Wüthrich, K. (1989) Biochemistry 28, 4312–4317.
Static and transient hydrogen-bonding interactions in recombinant desulfatohirudin studied by ¹H nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts.

339. Güntert, P., Braun, W., Billeter, M. and Wüthrich, K. (1989) J. Am. Chem. Soc. 111, 3997–4004.
Automated stereospecific ¹H NMR assignments and their impact on the precision of protein structure determinations in solution.

340. Senn, H., Werner, B., Messerle, B.A., Weber, C., Traber, R. and Wüthrich, K. (1989) FEBS Lett. 249, 113–118.
Stereospecific assignment of the methyl ¹H NMR lines of valine and leucine in polypeptides by nonrandom ¹³C labelling.

341. Schaumann, T., Braun, W. and Wüthrich, K. (1990) Biopolymers 29, 679–694.
The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space.

342. Billeter, M., Schaumann, T., Braun, W. and Wüthrich, K. (1990) Biopolymers 29, 695–706.
Restrained energy refinement with two different algorithms and force fields of the structure of the a-amylase inhibitor tendamistat determined by NMR in solution.

343. Bösch, C., Grütter, R., Martin, E., Duc, G. and Wüthrich, K. (1989) Radiology 172, 197–199.
Variations in the in vivo P-31 MR spectra of the developing human brain during postnatal life.

344. Neri, D., Szyperski, T., Otting, G., Senn, H. and Wüthrich, K. (1989) Biochemistry 28, 7510–7516.
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional ¹³C labeling.

345. Wüthrich, K. (1988) in Proceedings of the 8th International Biotechnology Symposium, (G.Durand, L. Bobichon and J. Florent, eds.) pp. 270–278, Société Française de Microbiologie, Paris.
Protein structure determination by nuclear magnetic resonance in solution.

346. Billeter, M. and Wüthrich, K. ((1989) in Computer-Aided Molecular Design, (W.G. Richards, ed.) pp. 197–201, IBC Technical Services Ltd., Oxford.
Interactive computer graphics for the determination of biopolymer conformations from NMR data measured in solution.

347. Qian, Y.Q., Billeter, M., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1989) Cell 59, 573–580.
The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors.

348. Widmer, H., Billeter, M. and Wüthrich, K. (1989) Proteins 6, 357–371.
Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy.

349. Wider, G., Neri, D., Otting, G. and Wüthrich, K. (1989) J. Magn. Reson. 85, 426–431.
heteronuclear three-dimensional NMR experiment for measurements of small heteronuclear coupling constants in biological macromolecules.

350. Wüthrich, K. (1989) Chemica Scripta 29A, 23–26.
Three-dimensional structures of non-crystalline proteins observed by nuclear magnetic resonance.

351. Otting, G. and Wüthrich, K. (1989) J. Magn. Reson. 85, 586–594.
Extended heteronuclear editing of 2D ¹H NMR spectra of isotope-labeled proteins, using the X(w₁,w₂)-double-half-filter.

352. Neri, D., Otting, G. and Wüthrich, K. (1990) Tetrahedron 46, 3287–3296.
¹H and ¹³C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins.

353. Messerle, B.A., Wider, G., Otting, G., Weber, C. and Wüthrich, K. (1989) J. Magn. Reson. 85, 608–613.
Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H₂O solutions.

354. Otting, G. and Wüthrich, K. (1990) Q. Rev. Biophys. 23, 39–96.
Heteronuclear filters in two-dimensional [¹H,¹H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions.

355. Billeter, M., Qian, Y.Q., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1990) J. Mol. Biol. 214, 183–197.
Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by ¹H nuclear magnetic resonance spectroscopy.

356. Messerle, B.A., Schäffer, A., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1990) J. Mol. Biol. 214, 765–779.
Three-dimensional structure of human [¹¹³Cd₇]-metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.

357. Messerle, B.A., Bos, M., Schäffer, A., VaÚs ák, M., Kägi, J.H.R. and Wüthrich, K. (1990) J. Mol. Biol. 214, 781–786.
Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy.

358. Wüthrich, K. (1989) Methods in Enzymology 177, 125–131.
Determination of three-dimensional protein structures in solution by nuclear magnetic resonance: an overview.

359. Otting, G. and Wüthrich, K. (1990) in Water and Ions in Biomolecular Systems (D. Vasilescu, J.Jaz, L. Packer and B. Pullman, eds.) pp. 141–147, Birkhäuser, Basel.
Studies of protein hydration by direct NMR observation of individual protein-bound water molecules.

360. Neri, D., Otting, G. and Wüthrich, K. (1990) J. Am. Chem. Soc. 112, 3663–3665.
New nuclear magnetic resonance experiment for measurements of the vicinal coupling constants ³J_HNa in proteins.

361. Leupin, W., Otting, G., Amacker, H. and Wüthrich, K. (1990) FEBS Lett. 263, 313–316.
Application of ¹³C(w_l )-half-filtered [¹H,¹H]-NOESY for studies of a complex formed between DNA and a ¹³C-labeled minor-groove-binding drug.

362. Wüthrich, K. (1990) Biochem. Pharmacol. 40, 55–62.
Structure and dynamics in proteins of pharmacological interest.

363. Wüthrich, K. (1989) in Protein Structure and Engineering, (O. Jardetzky, ed.) NATO ASI Series: Life Sciences A183, 69–78.
NMR method for protein structure determination in solution.

364. Grütter, R., Bösch, Ch., Müri, M., Martin, E. and Wüthrich, K. (1990) Magn. Reson. in Medicine 15, 128–134.
A simple design for a double-tunable probe head for imaging and spectroscopy at high fields.

365. Otting, G., Orbons, L.P.M. and Wüthrich, K. (1990) J. Magn. Reson. 89, 423–430.
Suppression of zero-quantum coherence in NOESY and soft-NOESY.

366. Vendrell, J., Wider, G., Avilés, F.X. and Wüthrich, K. (1990) Biochemistry 29, 7515–7522.
Sequence-specific ¹H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.

367. Gehring, W.J., Müller, M., Affolter, M., Percival-Smith, A., Billeter, M., Qian, Y.Q., Otting, G.and Wüthrich, K. (1990) Trends in Genetics 6, 323–329.
The structure of the homeodomain and its functional implications.

368. Otting, G., Qian, Y.Q., Billeter, M., Müller, M., Affolter, M., Gehring, W.J. and Wüthrich, K. (1990) EMBO J. 9, 3085–3092.
Protein–DNA contacts in the structure of a homeodomain–DNA complex determined by nuclear magnetic resonance spectroscopy in solution.

369. Wüthrich, K. (1990) Current Science 59, 825–831.
The Ramachandran plot and the NMR method for protein structure determination.

370. Wider, G., Weber, C., Traber, R., Widmer, H. and Wüthrich, K. (1990) J. Am. Chem. Soc. 112, 9015–9016.
Use of a double-half-filter in two-dimensional ¹H nuclear magnetic resonance studies of receptor-bound cyclosporin.

371. Wüthrich, K. (1990) J. Biol. Chem. 265, 22059–22062.
Protein structure determination in solution by NMR spectroscopy.

372. Vendrell, J., Billeter, M., Wider, G., Avilés, F.X. and Wüthrich, K. (1991) EMBO J. 10, 11–15.
The NMR structure of the activation domain isolated from porcine procarboxypeptidase B.

373. Grütter, R., Bösch, C., Martin, E. and Wüthrich, K. (1990) NMR in Biomedicine 3, 265–271.
A method for rapid evaluation of saturation factors in in vivo surface coil NMR spectroscopy using B₁-insensitive pulse cycles.

374. Güntert, P., Braun, W. and Wüthrich, K. (1991) J. Mol. Biol. 217, 517–530.
Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.

375. Güntert, P., Qian, Y.Q., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1991) J. Mol. Biol. 217, 531–540.
Structure determination of the Antp(C39®S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA.

376. Affolter, M., Percival-Smith, A., Müller, M., Billeter, M., Qian, Y.Q., Otting, G., Wüthrich, K. and Gehring, W.J. (1991) Cell 64, 879–880.
Similarities between the homeodomain and the hin recombinase DNA-binding domain.

377. Wüthrich, K. (1991) Japanese Edition of 'NMR of Proteins and Nucleic Acids' (translation by Y.Kyogoku and Y. Kobayashi). Kagaku Dozin, Tokyo, Japan.

378. Wider, G., Neri, D. and Wüthrich, K. (1991) J. Biomol. NMR 1, 93–98.
Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment.

379. Chary, K.V.R., Otting, G. and Wüthrich, K. (1991) J. Magn. Reson. 93, 218–224.
Measurement of small heteronuclear ¹H–¹⁵N coupling constants in ¹⁵N-labeled proteins by 3D H_NNH_AB-COSY.

380. Weber, C., Wider, G., von Freyberg, B., Traber, R., Braun, W., Widmer, H. and Wüthrich, K. (1991) Biochemistry 30, 6563–6574.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.

381. Otting, G., Liepinsh, E. and Wüthrich, K. (1991) J. Am. Chem. Soc. 113, 4363–4364.
Proton exchange with internal water molecules in the protein BPTI in aqueous solution.

382. Wider, G., Weber, C. and Wüthrich, K. (1991) J. Am. Chem. Soc. 113, 4676–4678.
Proton-proton Overhauser effects of receptor-bound cyclosporin A observed with the use of a heteronuclear-resolved half-filter experiment.

383. Wüthrich, K. (1991) in Proteins, Structure, Dynamics and Design (V. Renugopalakrishnan, P.R.Carey, I.C.P. Smith, S.G. Huang and A.C. Storer, eds.) pp. 3–10, ESCOM, Leiden.
NMR structures of proteins: Improved precision through stereospecific resonance assignments.

384. Eccles, C., Güntert, P., Billeter, M. and Wüthrich, K. (1991) J. Biomol. NMR 1, 111–130.
Efficient analysis of protein 2D NMR spectra using the software package EASY.

385. Neri, D., Billeter, M. and Wüthrich, K. (1992) J. Mol. Biol. 223, 743–767.
Determination of the NMR solution structure of the DNA-binding domain 1–69 of the 434 repressor and comparison with the X-ray crystal structure.

386. Otting, G., Liepinsh, E., Farmer II, B.T. and Wüthrich, K. (1991) J. Biomol. NMR 1, 209–215.
Protein hydration studied with homonuclear 3D ¹H NMR experiments.

387. Wüthrich, K., Spitzfaden, C., Memmert, K., Widmer, H. and Wider, G. (1991) FEBS Lett. 285, 237–247.
Protein secondary structure determination by NMR: application with recombinant human cyclophilin.

388. Sodano, P., Chary, K.V.R., Björnberg, O., Holmgren, A., Kren, B., Fuchs, J.A. and Wüthrich, K. (1991) Eur. J. Biochem. 200, 369–377.
Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin: sequence-specific assignments and secondary structure determination of the oxidized form.

389. Kallen, J., Spitzfaden, C., Zurini, M.G.M., Wider, G., Widmer, H., Wüthrich, K. and Walkinshaw, M.D. (1991) Nature 353, 276–279.
Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.

390. Mertz, J.E., Güntert, P., Wüthrich, K. and Braun, W. (1991) J. Biomol. NMR 1, 257–269.
Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities.

391. Wüthrich, K. (1991) in Protein Conformation, Ciba Foundation Symposium 161, pp. 136–149, Wiley, Chichester.
Six years of protein structure determination by NMR spectroscopy: What have we learned?

392. Sodano, P., Xia, T., Bushweller, J.H., Björnberg, O., Holmgren, A., Billeter , M. and Wüthrich, K. (1991) J. Mol. Biol. 221, 1311–1324.
Sequence-specific ¹H NMR assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.

393. Wüthrich, K., v. Freyberg, B., Weber, C., Wider, G., Traber, R., Widmer, H. and Braun, W. (1991) Science 254, 953–954.
Receptor-induced conformation change of the immunosuppressant cyclosporin A.

394. Otting, G., Liepinsh, E. and Wüthrich, K. (1991) Science 254, 974–980.
Protein hydration in aqueous solution.

395. Güntert, P. and Wüthrich, K. (1991) J. Biomol. NMR 1, 447–456.
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

396. Billeter, M., Vendrell, J., Wider, G., Avilés, F.X., Coll, M., Guasch, A., Huber , R. and Wüthrich, K. (1992) J. Biomol. NMR 2, 1–10.
Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B.

397. Montelione, G.T., Wüthrich, K., Burgess, A.W., Nice, E.C., Wagner, G., Gibson, D. and Scheraga, H.A. (1992) Biochemistry 31, 236–249.
Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.

398. Wüthrich, K. (1991) Methods in Enzymology 205, 502–520.
Determination of the three-dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution.

399. Spitzfaden, C., Weber, H.P., Braun, W., Kallen, J., Wider, G., Widmer, H., Walkinshaw, M.D. and Wüthrich, K. (1992) FEBS Lett. 300, 291–300.
Cyclosporin A–cyclophilin complex formation. A model based on X-ray and NMR data.

400. Wüthrich, K. and Otting, G. (1992) Int. J. Quant. Chem. 42, 1553–1561.
Studies of protein hydration in aqueous solution by high-resolution nuclear magnetic resonance spectroscopy.

401. Otting, G., Liepinsh, E. and Wüthrich, K. (1992) J. Am. Chem. Soc. 114, 7093–7095.
Polypeptide hydration in mixed solvents at low temperatures.

402. Güntert, P. and Wüthrich, K., (1992) J. Magn. Reson. 96, 403–407.
FLATT¾A new procedure for high-quality baseline correction of multidimensional NMR spectra.

403. Neri, D., Wider, G. and Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 4397–4401.
Complete ¹⁵N and ¹H NMR assignments for the amino-terminal domain of the phage434 repressor in the urea-unfolded form.

404. Xia, T., Bushweller, J.H., Sodano, P., Billeter, M., Björnberg, O., Holmgren, A. and Wüthrich, K. (1992) Protein Science 1, 310–321.
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.

405. Billeter, M., Neri, D., Otting, G., Qian, Y.Q. and Wüthrich, K., (1992) J. Biomol. NMR 2, 257–274.
Precise vicinal coupling constants ³J_HNa in proteins from nonlinear fits of J-modulated [¹⁵N,¹H]-COSY experiments.

406. Neri, D., Wider , G. and Wüthrich, K. (1992) FEBS Lett. 303, 129–135.
¹H, ¹⁵N and ¹³C NMR assignments of the 434 repressor fragments 1–63 and 44–64 unfolded in 7 M urea.

407. Messerle, B.A., Schäffer, A., Vašák, M., Kägi, J.H.R. and Wüthrich, K. (1992) J. Mol. Biol. 225, 433–443.
Comparison of the solution conformations of human [Zn₇]-metallothionein-2 and [Cd₇]-metallothionein-2 using nuclear magnetic resonance spectroscopy.

408. Szyperski, T., Neri, D., Leiting, B., Otting, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 323–334.
Support of ¹H NMR assignments in proteins by biosynthetically directed fractional ¹³C-labeling.

409. Liepinsh, E., Otting, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 447–465.
NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.

410. Vendrell, J., Guasch, A., Coll, M., Villegas, V. Billeter, M., Wider, G., Huber, R., Wüthrich, K. and Avilés, F. (1992) Biol. Chem. Hoppe-Seyler 373, 387–392.
Pancreatic procarboxypeptidases: their activation processes related to the structural features of the zymogens and activation segments.

411. Berndt, K.D., Güntert, P., Orbons, L.P.M. and Wüthrich, K. (1992) J. Mol. Biol. 227, 757–775.
Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures.

412. Szyperski, T., Güntert, P., Otting, G. and Wüthrich, K. (1992) J. Magn. Reson. 99, 552–560.
Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets.

413. Bushweller, J.H., Åslund, F., Wüthrich, K. and Holmgren, A. (1992) Biochemistry 31, 928–293.
Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14®S) and its mixed disulfide with glutathione.

414. Brown, L.R. and Wüthrich, K. (1992) J. Mol. Biol. 227, 1118–1135.
Nuclear magnetic resonance solution structure of the a-neurotoxin from the black mamba (Dendroaspis polylepis polylepis).

415. Neri, D., Billeter, M., Wider, G. and Wüthrich, K. (1992) Science 257, 1559–1563.
NMR determination of residual structure in a urea-denatured protein, the 434 repressor.

416. Wüthrich, K., Szyperski, T., Leiting, B. and Otting, G., (1992) in Frontiers and New Horizons in Amino Acid Research (Proc. 1st Biennial International Conference on Amino Acid Research, Frontiers and Horizons, K. Takai, ed.), pp.41–48, Elsevier, Amsterdam.
Biosynthetic pathways of the common proteinogenic amino acids investigated by fractional ¹³C labeling and NMR spectroscopy.

417. Wüthrich, K., Otting, G. and Liepinsh, E. (1992) Faraday Discuss. 93, 35–45.
Protein hydration in aqueous solution.

418. Braun, W., Vašák, M., Robbins, A.H., Stout, C.D., Wagner, G., Kägi, J.H.R. and Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 10124–10128.
Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2.

419. Qian, Y.Q., Otting, G., Furukubo-Tokunaga, K., Affolter, M., Gehring, W.J. and Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 10738–10742.
NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein.

420. Güntert, P., Dötsch, V., Wider, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 619–629.
Processing of multi-dimensional NMR data with the new software PROSA.

421. Liepinsh, E., Otting, G. and Wüthrich, K. (1992) Nucl. Acids Res. 20, 6549–6553.
NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.

422. Szyperski, T. Güntert, P., Stone, S.R. and Wüthrich, K. (1992) J. Mol. Biol. 228, 1193–1205.
Nuclear magnetic resonance solution structure of hirudin(1–51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain.

423. Szyperski, T., Güntert, P., Stone, S.R., Tulinsky, A., Bode, W., Huber, R. and Wüthrich, K. (1992) J. Mol. Biol. 228, 1206–1211.
Impact of protein–protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1–51).

424. Wüthrich, K. (1992) Nova acta Leopoldina NF 60, Nr. 266, 47–56.
Strukturermittlung an Proteinen und Nukleinsäuren in Lösung mittels NMR.

425. Wüthrich, K. and Gehring, W.J. (1992) in Transcriptional Regulation (S.L. McKnight and K.R. Yamamoto, eds.) pp. 535–577, Cold Spring Harbor Laboratory Press, Plainview, NY, USA.
Transcriptional regulation by homeodomain proteins: structural, functional, and genetic aspects.

426. Szyperski, T., Wider, G., Bushweller, J.H. and Wüthrich, K. (1993) J. Biomol. NMR 3, 127–132.
3D ¹³C–¹⁵N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in ¹³C–¹⁵N-double-labeled proteins.

427. Qian, Y.Q., Otting, G. and Wüthrich, K. (1993) J. Am. Chem. Soc. 115, 1189–1190.
NMR detection of hydration water in the intermolecular interface of a protein–DNA complex.

428. Wüthrich, K., Otting, G., Qian, Y.Q., Billeter, M. and Gehring, W. (1992) in Molecular Structure and Life (Y. Kyogoku and Y. Nishimura, eds.), pp.115–127, Japan Scientific Societies Press, Tokyo.
Molecular recognition in the homeodomain–DNA system.

429. Güntert, P., Schaefer, N., Otting, G. and Wüthrich, K. (1993) J. Magn. Reson. 101, 103–105.
POMA: A complete Mathematica implementation of the NMR product-operator formalism.

430. Leiting, B., de Francesco, R., Tomei, L., Cortese, R., Otting, G. and Wüthrich, K. (1993) EMBO J. 12, 1797–1803.
The three-dimensional NMR-solution structure of the polypeptide fragment 195–286 of the LFB1/HNF1 transcription factor from rat liver comprises a non-classical homeodomain.

431. Brown, L.R., Mronga, S., Bradshaw, R.A., Ortenzi, C., Luporini, P. and Wüthrich, K. (1993) J.Mol. Biol. 231, 800–816.
Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi.

432. Berndt, K.D., Beunink, J., Schröder, W. and Wüthrich, K. (1993) Biochemistry 32, 4564–4570.
Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a Gly-to-Ser mutation.

433. Otting, G., Liepinsh, E. and Wüthrich, K. (1993) Biochemistry 32, 3571–3582.
Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.

434. Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. and Wüthrich, K. (1993) J. Biomol. NMR 3, 151–164.
Protein dynamics studied by rotating frame ¹⁵N spin relaxation times.

435. Liepinsh, E., Rink, H., Otting, G. and Wüthrich, K. (1993) J. Biomol. NMR 3, 253–257.
Contribution from hydration of carboxylate groups to the spectrum of water–polypeptide proton–proton Overhauser effects in aqueous solution.

436. Gehring, W.J. and Wüthrich, K. (1993) Structure 0, IV–V.
Structural and functional analysis of homeodomain–DNA interactions.

437. Antuch, W., Berndt, K.D., Chavez, M.A., Delfin, J. and Wüthrich, K. (1993) Eur. J. Biochem. 212, 675–684.
The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus.

438. O’Connell, J.F., Bougis, P.E. and Wüthrich, K. (1993) Eur. J. Biochem. 213, 891–900.
Determination of the nuclear-magnetic-resonance solution structure of cardiotoxin CTX IIb from Naja mossambica mossambica.

439. Wüthrich, K., Güntert, P. and Berndt, K.D. (1993) in Innovations in Proteases and their Inhibitors (F.X. Avilés, ed.) pp. 407–424, Walter de Gruyter, Berlin.
Computer-supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors.

440. Berndt, K.D., Güntert, P. and Wüthrich, K. (1993) J. Mol. Biol. 234, 735–750.
Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis.

441. Qian, Y.Q., Otting, G., Billeter, M., Müller, M., Gehring, W.J. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1070–1083.
Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformly ¹³C-labeled Antennapedia homeodomain and structure determination of the DNA-bound homeodomain.

442. Billeter, M., Qian, Y.Q., Otting, G., Müller, M. Gehring, W. J. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1084–1093.
Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain–DNA complex.

443. Billeter, M. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1094–1097.
Model Studies relating nuclear magnetic resonance data with the three-dimensional structure of protein–DNA complexes.

444. Brunne, R.M., Liepinsh, E., Otting, G., Wüthrich, K. and van Gunsteren, W.F. (1993) J. Mol. Biol. 231, 1040–1048.
Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations.

445. Güntert, P., Berndt, K.D. and Wüthrich, K. (1993) J. Biomol. NMR 3, 601–606.
The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination.

446. Wider, G. and Wüthrich, K. (1993) J. Magn. Reson. B 102, 239–.
A simple experimental scheme using pulsed field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra.

447. Fede, A., Billeter, M., Leupin, W. and Wüthrich, K. (1993) Structure 1, 177–186.
Determination of the NMR solution structure of the Hoechst 33258– d(GTGGAATTCCAC)₂ complex and comparison with the X-ray crystal structure.

448. Szyperski, T., Scheek, S., Johansson, J., Assmann, G., Seedorf, U. and Wüthrich, K. (1993) FEBS Lett. 335, 18–26.
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.

449. Szyperski, T., Wider, G. Bushweller, J.H. and Wüthrich, K. (1993) J. Am. Chem. Soc. 115, 9307–9308.
Reduced dimensionality in triple-resonance NMR experiments.

450. Wüthrich, K. (1993) in Molecular Structures in Biology (R. Diamond, T.F. Koetzle, K. Prout and J.S.Richarsdon, eds.) pp. 20–26, Oxford Univ. Press, Oxford.
Biopolymers: an NMR survey.

451. Otting, G., Billeter, M., Wüthrich, K., Roth, H.J., Leumann, C. and Eschenmoser, A. (1993) Helv. Chim. Acta 76, 2701–2756.
Warum Pentose- und nicht Hexose-Nucleinsäuren? ‘Homo-DNS’: ¹H-, ¹³C-, ³¹P- und ¹⁵N-NMR-spektroskopische Untersuchung von ddGlc(A-A-A-A-A-T-T-T-T-T) in wässriger Lösung

452. Bushweller, J.H., Holmgren, A. and Wüthrich, K. (1993) Eur. J. Biochem. 218, 327–334.
Biosynthetic ¹⁵N and ¹³C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.

453. Wüthrich, K. (1994) Current Opinion in Structural Biology 4, 93–99.
NMR assignment as a basis for structural characterization of denatured states of globular proteins.

454. Sevilla-Sierra, P., Otting, G. and Wüthrich, K. (1994) J. Mol. Biol. 235, 1003–1020.
Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor.

455. Wüthrich, K. (1993) Les Cahiers de la Fondation, Vol. 8, Fondation Louis Jeantet de Médecine, Genève, Suisse.
Three-dimensional protein structures in biological and biomedical research.

456. Bushweller, J.H., Billeter, M., Holmgren, A. and Wüthrich, K. (1994) J. Mol. Biol. 235, 1585–1597.
The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.

457. Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K. and Plückthun, A. (1994) Nature 368, 261–265.
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

458. O’Connell, J.F., Bender, R., Engels, J.W., Koller, K.P., Scharf, M. and Wüthrich, K. (1994) Eur. J. Biochem. 220, 763–770.
The nuclear-magnetic-resonance solution structure of the mutant a-amylase inhibitor [R19L]Tendamistat and comparison with wild-type Tendamistat.

459. Leupin, W., Bur, D., Dorn, A., Ji, Y.H., Labhardt, A., Fede, A., Billeter, M. and Wüthrich, K. (1994) Actual. Chim. Thér. 21, 153–170.
Bis-benzimidazole derivatives as DNA ligands: design based on the solution structure of a Hoechst 33258–DNA complex with subsequent molecular modelling.

460. Wüthrich, K. (1994) in Toward a Molecular Basis of Alcohol Use and Abuse (B. Jansson, H.Jörnvall, U. Rydberg, L. Terenius and B.L. Vallee, eds.) pp. 261–268, Birkhäuser Verlag, Basel.
NMR, alcohols, protein solvation and protein denaturation.

461. Qian, Y.Q., Furukubo-Tokunaga, K., Resendez-Perez, D., Müller, M., Gehring, W.J. and Wüthrich K. (1994) J. Mol. Biol. 238, 333–345.
Nuclear magnetic resonance solution structure of the fushi tarazu homeodomain from Drosophila and comparison with the Antennapedia homoedomain.

462. Qian, Y.Q., Resendez-Perez, D., Gehring, W.J. and Wüthrich, K. (1994) Proc. Natl. Acad. Sci. USA 91, 4091–4095.
The des(1–6)Antennapedia homeodomain: comparison of the NMR solution structure and the DNA-binding affinity with the intact Antennapedia homeodomain.

463. Wüthrich, K. (1993) in DNA and Chromosomes, Cold Spring Harbor Symposia on Quantitative Biology 58, 149–157.
Hydration of biological macromolecules in solution: surface structure and molecular recognition.

464. Johansson, J., Szyperski, T., Curstedt, T. and Wüthrich, K. (1994) Biochemistry 33, 6015– 6023.
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich a-helix.

465. Wider, G., Dötsch, V. and Wüthrich, K. (1994) J. Magn. Reson. A 108, 255–258.
Self-compensating pulsed magnetic-field gradients for short recovery times.

466. Spitzfaden, C., Braun, W., Wider, G., Widmer, H. and Wüthrich K. (1994) J. Biomol. NMR 4, 463–482.
Determination of the NMR solution structure of the cyclophilin A–cyclosporin A complex.

467. Szyperski, T., Antuch, W., Schick, M., Betz, A., Stone, S.R. and Wüthrich, K. (1994) Biochemistry 33, 9303–9310.
Transient hydrogen bonds identified on the surface of the NMR solution structure of hirudin.

468. Ottiger, M., Szyperski, T., Luginbühl, L., Ortenzi, C., Luporini, P., Bradshaw, R.A. and Wüthrich, K. (1994) Protein Science 3, 1515–1526.
The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi.

469. Mronga, S., Luginbühl, P., Brown, L.R., Ortenzi, C., Luporini, P., Bradshaw R.A. and Wüthrich, K. (1994) Protein Science 3, 1527–1536.
The NMR solution structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.

470. Luginbühl, P., Ottiger, M., Mronga, S. and Wüthrich, K. (1994) Protein Science 3, 1537– 1546.
Structure comparison of the pheromones Er-1, Er-10, and Er-2 from Euplotes raikovi.

471. Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. and Wüthrich, K. (1994) FEBS Lett. 352, 251–257.
NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor XA inhibitor from the tick Ornithodoros moubata.

472. Szyperski, T., Pellecchia, M., Wall, D., Georgopoulos, C. and Wüthrich, K. (1994) Proc. Natl. Acad. Sci. USA 91, 11343–11347.
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region 2–108 comprising the highly conserved J-domain.

473 Gehring, W.J., Qian, Y.Q., Billeter, M., Furukubo-Tokunaga, K., Schier, A. F., Resendez-Perez, D., Affolter, M., Otting, G. and Wüthrich, K. (1994) Cell, 78, 211–223.
Homeodomain–DNA recognition.

474. Dötsch, V., Wider, G. and Wüthrich, K. (1994) J. Magn. Reson. A 109, 263–264.
Phase-sensitive spectra in a single scan with coherence selection by pulsed field gradients.

475. Schiffer, C.A., Huber, R., Wüthrich, K. and van Gunsteren, W.F. (1994) J. Mol. Biol. 241, 588–599.
Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X‑ray diffraction data measured in single crystals.

476. Braun, D., Wider, G. and Wüthrich, K. (1994) J. Am. Chem. Soc. 116, 8466–8469.
Sequence-corrected ¹⁵N “Random Coil” chemical shifts.

477. Szyperski, T., Pellecchia, M. and Wüthrich, K. (1994) J. Magn. Reson. B 105, 188–191.
3D H^a/bC^a/b(CO)NHN, a projected 4D NMR experiment for sequential correlation of polypeptide ¹H^a/b, ¹³C^a/b and backbone ¹⁵N and ¹H^N chemical shifts.

478. Bartels, C. and Wüthrich, K. (1994) J. Biomol. NMR 4, 775–785.
A spectral correlation function for efficient sequential NMR assignments of uniformly ¹⁵N-labeled proteins.

479. Altschuh, D., Braun, W., Kallen, J., Mikol, V., Spitzfaden, C., Thierry, J.C., Vix, O., Walkinshaw, M.D. and Wüthrich, K. (1994) Structure 2, 963–972.
Conformational polymorphism of cyclosporin A.

480. Smith, P.E., van Schaik, R.C., Szyperski, T., Wüthrich, K. and van Gunsteren, W.F. (1995) J. Mol. Biol. 246, 356–365.
Internal mobility of the basic pancreatic trypsin inhibitor in solution: A comparison of NMR spin relaxation measurements and molecular dynamics simulations.

481. Braun, W., Kallen, J., Mikol, V., Walkinshaw, M.D. and Wüthrich K. (1995) FASEB Journal 9, 63–72.
Three-dimensional structure and actions of immunosuppressants and their immunophilins.

482. Johansson, J., Szyperski, T. and Wüthrich, K. (1995) FEBS Lett. 362, 261–265.
Pulmonary surfactant-associated polypeptide SP-C in lipid micelles: CD studies of intact SP-C and NMR secondary structure determination of depalmitoyl-SP-C(1–17).

483. Wüthrich, K. (1995) Acta Cryst. D 51, 249–270.
NMR–this other method for protein and nucleic acid structure determination.

484. Wüthrich, K. (1995) in Proc. XIIIth International Symposium on Medical Chemistry (J.C. Muller, ed.) Eur. J. Med. Chem. 30, 68s–84s.
Structure determination of biological macromolecules by NMR in solution: Impact in biomedical research.

485. Dötsch, V., Wider, G., Siegal, G. and Wüthrich, K. (1995) FEBS Lett. 366, 6–10.
Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor.

486. Wüthrich, K. (1995) NMR in Structural Biology, World Scientific, Singapore.

487. Szyperski, T., Braun, D., Fernández, C., Bartels, C. and Wüthrich K. (1995) J. Magn. Reson. B 108, 197–203.
A novel reduced-dimensionality triple-resonance experiment for efficient polypeptide backbone assignment, 3D CO HN N CA.

488. Bartels, C., Xia, T., Billeter, M., Güntert, P. and Wüthrich K. (1995) J. Biomol. NMR 6, 1– 10.
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.

489. Dötsch, V., Wider, G., Siegal, G. and Wüthrich, K. (1995) FEBS Lett. 372, 288–290.
Salt-stabilized globular protein structure in 7M aqueous urea solution.

490. Brunne, R.M., Berndt, K.D., Güntert, P., Wüthrich, K. and van Gunsteren, W.F. (1995) Proteins 23, 49–62.
Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations.

491. Luginbühl, P., Szyperski, T. and Wüthrich, K. (1995) J. Magn. Reson. B 109, 229–233.
Statistical basis for the use of ¹³C^a chemical shifts in protein structure determination.

492. Schiffer, C.A., Dötsch, V., Wüthrich, K. and van Gunsteren, W. (1995) Biochemistry 34, 15057–15067.
Exploring the role of the solvent in the denaturation of a protein: A molecular dynamics study of the DNA binding domain of the 434 repressor.

493. Altmann, S., Labhardt, A.M., Bur, D., Lehmann, C., Bannwarth, W., Billeter, M., Wüthrich, K. and Leupin, W. (1995) Nucl. Acids Res. 23, 4827–4835.
NMR studies of DNA duplexes singly cross-linked by different synthetic linkers.

494. Bartels, C., Güntert, P. and Wüthrich, K. (1995) J. Magn. Reson. A 117, 330–333.
IFLAT – A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals.

495. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 1, pp. 710–719.
NMR structures of biological macromolecules.

496. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 2, pp. 932–939.
Biological macromolecules: structure determination in solution.

497. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 5, pp. 3449–3455.
Pancreatic trypsin inhibitor.

498. Berndt, K.D., Güntert, P. and Wüthrich, K. (1996) Proteins 3, 304–313.
Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water.

499. Koradi, R, Billeter, M. and Wüthrich, K (1996) J. Mol. Graph. 14, 51–55.
MOLMOL: a program for display and analysis of macromolecular structures.

500. Zerbe, O., Szyperski, T., Ottiger, M. and Wüthrich, K. (1996) J. Biomol. NMR 7, 99–106.
Three-dimensional ¹H-TOCSY-relayed ct-[¹³C,¹H]-HMQC for aromatic spin system identification in uniformly ¹³C labeled proteins.

501. Braun, D., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. B 110, 313–315.
Monitoring NMR spectrometer performance during data accumulation for macromolecular structure determination.

502. Bartels, C., Billeter, M., Güntert, P. and Wüthrich, K. (1996) J. Biomol. NMR 7, 207–213.
Automated sequence-specific NMR assignment of homologous proteins using the program GARANT.

503. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wüthrich, K. (1996) Nature 382, 180–182.
NMR structure of the mouse prion protein domain PrP(121–231).

504. Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C. and Wüthrich, K. (1996) J. Mol. Biol. 260, 236–250.
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.

505. Billeter, M., Güntert, P., Luginbühl, P. and Wüthrich, K. (1996) Cell 85, 1057–1065.
Hydration and DNA recognition by homeodomains.

506. Kupce, E., Freeman, R., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. A 120, 264– 268.
Figure of merit and cycling sidebands in adiabatic decoupling.

507. Antuch, W., Güntert, P. and Wüthrich, K. (1996) Nature Struct. Biol. 3, 662–665.
Ancestral bg-crystallin percursor structure in a yeast killer toxin.

508. Luginbühl, P., Wu, J., Zerbe, O., Ortenzi, C., Luporini, P. and Wüthrich, K. (1996) Protein Science 5, 1512–1522.
The NMR solution structure of the pheromone Er-11 from the cilitated protozoan Euplotes raikovi.

509. Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G. and Wüthrich, K. (1996) Spektrum der Wissenschaften 9, 16–18.
Dreidimensionale Struktur einer Domäne des zellulären Prion-Proteins aufgeklärt.

510. Szypersky, T., Bailey, J.E. and Wüthrich, K. (1996) Trends Biotechn. 14, 453–459.
Detecting and dissecting metabolic fluxes using biosynthetic fractional ¹³C-labeling and two-dimensional NMR spectroscopy.

511. Szyperski, T., Braun, D., Banecki, B. and Wüthrich, K. (1996) J. Am. Chem. Soc. 118, 8146–8147.
Useful information from axial peak magnetization in projected NMR experiments.

512. Wüthrich, K. (1996) in Molecular Manufacturing, EL.B.A. Forum Series, Vol. 2 (C. Nicolini and S. Vakula, eds.) pp. 115–130, Plenum Press, New York.
NMR structure determination and rational drug design.

513. Kupce, E., Freeman, R., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. A 122, 81–84.
Suppression of cycling sidebands using bi-level adiabatic decoupling.

514. Luginbühl, P., Güntert, P., Billeter, M. and Wüthrich, K. (1996) J. Biomol. NMR 8, 136– 146.
The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.

515. Wider, G., Riek R. and Wüthrich, K. (1996) J. Am. Chem. Soc. 118, 11629–11634.
Diffusion filters for separation of solvent–protein and protein–protein nuclear Overhauser effects (HYDRA).

516. Pervushin, K., Billeter, M., Siegal, G. and Wüthrich, K. (1996) J. Mol. Biol. 264, 1002– 1012.
Structural role of a buried salt bridge in the 434 repressor DNA-binding domain.

517. Bartels, C., Güntert, P., Billeter, M. and Wüthrich, K. (1997) J. Comp. Chem. 18, 139–149.
GARANT– a general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra.

518. Pellecchia, M., Iwai, H., Szyperski, T. and Wüthrich, K. (1997) J. Magn. Reson. 124, 274– 278.
The 2D NMR experiments H(C)CO₂ and HCCO₂ for assignment and pH titration of carboxylate groups in uniformly ¹⁵N/¹³C-labeled proteins.

519. Wüthrich, K. (1997) Chimia 51, 16–17.
Structural insight into prion diseases.

520. Fernández ,C., Szyperski, T., Bruyère, T., Ramage, P., Mösinger, E. and Wüthrich, K. (1997) J. Mol. Biol. 266, 576–593.
NMR solution structure of the pathogenesis-related protein P14a.

521. Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. and Wider, G. (1996) Faraday Discuss. 103, 245–253.
NMR studies of the hydration of biological macromolecules.

522. Schott, O., Billeter, M., Leiting, B., Wider, G. and Wüthrich, K. (1997) J. Mol. Biol. 267, 673–683.
The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.

523. Sauer, U., Hatzimanikatis, V., Bailey, J.E., Hochuli, M., Szyperski, T. and Wüthrich, K. (1997) Nature Biotech. 15, 448–452.
Metabolic fluxes in riboflavin-producing Bacillus subtilis.

524. Pervushin, K., Wider, G. and Wüthrich, K. (1997) J. Am. Chem. Soc. 119, 3842– 3843.
Deuterium relaxation in a uniformly ¹⁵N-labeled homeodomain and its DNA complex.

525. Luginbühl, P., Pervushin, K.V., Iwai, H. and Wüthrich, K. (1997) Biochemistry 36, 7305–7312.
Anisotropic molecular rotational diffusion in ¹⁵N spin relaxation studies of protein mobility.

526. Wüthrich, K. (1996) Proc. Natl. Acad. Sci. India 66, 1–8.
NMR for physicochemical characterization of proteins.

527. Wüthrich, K. (1997) in Röntgen Centennial: X-rays in Natural and Life Sciences (A. Haase, G. Landwehr and E. Umbach, eds.) pp. 242–257, World Scientific, Singapore.
NMR - an alternative to x-ray crystallography for protein and nucleic acid structure determination.

528. King, C.Y., Trittmann, P., Gross, H., Gebert, R., Aebi, M. and Wüthrich, K. (1997) Proc. Natl. Acad Sci. USA 94, 6618–6622.
Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments.

529. Billeter, M., Riek, R., Wider, G., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA 94, 7281–7285.
Prion protein NMR structure and species barrier for prion diseases.

530. Glockshuber, R., Hornemann S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1997) Trends Biochem. Sci. 22, 241–242.
Three-dimensional NMR structure of a self-folding domain of the prion protein PrP(121–231).

531. Altmann, S., Labhardt, A.M., Senn, H. and Wüthrich, K. (1997) J. Biomol. NMR 9, 445–446.
Sequence-specific 1H, 13C and 15N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH.

532. Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wüthrich, K. and Glockshuber, R. (1997) FEBS Lett. 413, 277–281.
Recombinant full-length murine prion protein, mPrP(23–231): purification and spectroscopic characterization.

533. Riek, R., Hornemann, S., Wider, G., Glockshuber, R. and Wüthrich, K. (1997) FEBS Lett. 413, 282–288.
NMR characterization of the full length recombinant murine prion protein, mPrP(23–231).

534. Nieba-Axmann, S. E., Ottiger, M., Wüthrich, K. and Plückthun, A. (1997) J. Mol. Biol. 271, 803–818.
Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

535. Ottiger, M., Zerbe, O., Güntert, P. and Wüthrich, K. (1997) J. Mol. Biol. 272, 64–81.
The NMR solution conformation of unligated human cyclophilin A.

536. Güntert, P., Mumenthaler, C. and Wüthrich, K. (1997) J. Mol. Biol. 273, 283–298.
Torsion angle dynamics for NMR structure calculation with the new program DYANA.

537. Pellecchia, M., Wider, G., Iwai, H. and Wüthrich, K. (1997) J. Biomol. NMR 10, 193–197.
Arginine side chain assignments in uniformly ¹⁵N-labeled proteins using the novel 2D HE(NE)HGHH experiment.

538. Klimasauskas, S., Szyperski, T., Serva, S. and Wüthrich, K. (1998) EMBO J. 17, 317–324.
Dynamic modes of the flipped-out cytosine during HhaI methyltransferase–DNA interactions in solution.

539. Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA 94, 12366–12371.
Attenuated T₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution.

540. Korth, C., Stierli, E., Streit, P., Moser, M., Schaller, O., Fischer, R., Schulz-Schaeffer, W., Kretschmar, H., Raeber, A., Braun, U., Ehrensperger, F., Hornemann, S., Glockshuber, R., Riek, R., Billeter, M., Wüthrich, K. and Oesch, B. (1997) Nature 390, 74–77.
Prion (PrP^Sc)-specific epitope defined by a monoclonal antibody.

541. Szyperski, T., Ono A., Fernández C., Iwai H., Tate, S., Wüthrich, K. and Kainosho, M. (1997) J.Am. Chem. Soc. 119, 9901–9902.
Measurement of ³J_C2’P scalar couplings in a 17 kDa protein complex with ¹³C,¹⁵N-labeled DNA distinguishes the B_I and B_II phosphate conformations of the DNA.

542. Zahn, R., von Schroetter C. and Wüthrich, K. (1997) FEBS Lett. 417, 400–404.
Human prion proteins expressed in Echerichia coli and purified by high-affinity column refolding.

543. Szyperski, T., Férnandez C. and Wüthrich K. (1997) J. Magn. Reson. 128, 228–232.
Two-Dimensional ct-HC(C)H-COSY for resonance assignments of smaller ¹³C-labeled biomolecules.

544. Mumenthaler, C., Güntert, P., Braun, W. and Wüthrich, K. (1997) J. Biomol. NMR 10, 351– 362.
Automated combined assignment of NOESY spectra and three-dimensional protein structure determination.

545. Glockshuber, R., Hornemann, S., Billeter, M., Riek, R., Wider, G., and Wüthrich, K. (1998) FEBS Lett. 426, 291–296.
Prion protein structural features indicate possible relations to signal peptidases.

546. Szyperski, T., Férnandez, C., Ono, A., Kainosho, M. and Wüthrich, K. (1998) J. Am. Chem. Soc. 120, 821–822.
Measurement of deoxyribose ³J_HH scalar couplings reveals protein binding-induced changes in the sugar puckers of the DNA.

547. Szyperski, T., Férnandez, C., Mumenthaler, C. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 2262–2266.
Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system.

548. Sobol, A. G., Wider, G., Iwai, H. and Wüthrich, K. (1998) J. Magn. Reson. 130, 262–271.
Solvent magnetization artifacts in high-field NMR studies of macromolecular hydration.

549. Pellecchia, M., Güntert, P., Glockshuber, R. and Wüthrich, K. (1998) J. Biomol. NMR 11, 229–230.
Sequence-specific ¹H, ¹⁵N and ¹³C assignments of the periplasmic chaperone FimC from Escherichia coli.

550. Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1998) J. Am. Chem. Soc. 120, 6394– 6400.
Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in ¹³C-labeled proteins.

551. Wüthrich, K. (1998) Nature Struct. Biol. 5, 492–495.
The second decade – into the third millenium.

552. Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes. B. D., Wright, P. E. and Wüthrich, K. (1998) Pure Appl. Chem. 70, 117–142; reprinted: (1998) J. Biomol NMR, 12, 1–23; (1998) J. Mol. Biol. 280, 933–952.
Recommendations for the presentation of NMR structures of proteins and nucleic acids.

553. Glockshuber, R., Hornemann, S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1998) in NATO ASI Series A: Life Sciences (D. R. O. Morrison, ed.) vol. 295, pp. 203–216.
Autonomous folding and three-dimensional structure of the carboxy-terminal domain of the mouse prion protein, PrP(121–231).

554. Weber, F. E., Dyer, J. H., Lopez Garcia, F., Werder, M., Szyperski, T., Wüthrich, K. and Hauser, H. (1998) Cell. Mol. Life Sci. 54, 751–759.
In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1–20 is flexibly disordered, and residues 21–143 adopt the same globular fold as in mature SCP2.

555. Pervushin, K. V., Wider, G. and Wüthrich, K. (1998) J. Biomol. NMR 12, 345–348.
Single transition-to-single transition polarization transfer (ST2-PT) in [¹⁵N,¹H]-TROSY.

556. Fernàndez C., Szyperski, T., Ono, A., Iwai, H., Tate, S., Kainosho, M. and Wüthrich, K. (1998) J. Biomol. NMR 12, 25–37.
NMR with ¹³C,¹⁵N-doubly-labeled DNA: The Antennapedia homeodomain complex with a 14-mer DNA duplex.

557. Pellecchia, M., Güntert, P., Glockshuber R. and Wüthrich, K. (1998) Nature Struct. Biol. 5, 10, 885–890.
NMR solution structure of the periplasmic chaperone FimC.

558. Riek, R., Wider, G., Billeter, M., Hornemann, S., Glockshuber R. and Wüthrich K. (1998) Proc. Natl. Acad. Sci. USA 95, 11667–11672.
Prion protein NMR structure and familial human spongiform encephalopathies.

559. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 13585–13590
TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins.

560. Banci, L., Bertini, I., Cremonini, M.A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. and Güntert, P. (1998) J. Biomol. NMR 12, 553–557.
PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics.

561. Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L.R. and Wüthrich, K. (1998) J. Biomol. NMR 12, 543–548.
Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND.

562. Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G., Liemann, S., Zahn, R. and Wüthrich, K. (1998) in PRIONS - Molecular and Cellular Biology (D. A. Harris, ed.) Horizon Scientific Press, pp. 1–25.
Folding and three-dimensional NMR structure of the recombinant cellular prion protein from the mouse.

563. Pervushin, K., Ono, A., Fernandez, C., Szyperski, T., Kainosho, M. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 14147–14151.
NMR scalar couplings across Watson–Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.

564. Koradi, R., Billeter, M., Engeli, M., Güntert, P., and Wüthrich, K. (1998) J. Magn. Reson. 135, 288–297.
Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY.

565. Szyperski, T., Vandenbussche, G., Curstedt, T., Ruysschaert, J.-M., Wüthrich, K. and Johansson J. (1998) Protein Science 7, 2533–2540.
Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric a-helical state into insoluble b-sheet aggregates.

566. Salzmann, M., Wider, G., Pervushin, K., Senn, H. and Wüthrich, K. (1999) J. Am. Chem. Soc. 121, 844–848.
TROSY-type triple resonance experiments for sequential NMR assignments of large proteins.

567. Fiaux, J., Andersson, Ch.I.J., Holmberg, N., Bülow, L., Kallio, P.T., Szypersky, T., Bailey, J.E. and Wüthrich, K. (1999) J. Am. Chem. Soc. 121, 1407–1408.
¹³C NMR flux ratio analysis of Escherichia coli central carbon metabolism in microaerobic bioprocesses.

568. Pellecchia, M., Sebbel, P., Hermanns, U., Wüthrich, K. and Glockshuber, R. (1999) Nature Struct. Biol. 6, 336–339.
Pilus chaperone FimC–adhesin FimH interactions mapped by TROSY-NMR.

569. Fattorusso, R., Pellecchia, M., Viti, F., Neri. P., Neri, D. and Wüthrich, K. (1999) Structure with Folding and Design 7, 381–390.
NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis.

570. Szyperski, T., Götte, M., Billeter, M., Perola, E., Cellai, L., Heumann, H. and Wüthrich, K. (1999) J. Biomol. NMR 13, 343–355.
NMR structure of the chimeric hybrid duplex r(gcaguggc)•r(gcca)d(CTGC) comprising the tRNA-DNA junction formed during initiation of HIV-1 reverse transcription.

571. Riek, R., Wider, G., Pervushin, K. and Wüthrich, K. (1999) Proc. Natl. Acad. Sci. USA 96, 4918–4923.
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.

572. Hochuli, M., Patzelt, H., Oesterhelt, D., Wüthrich, K. and Szyperski, T. (1999) J. Bacteriol. 181, 3226–3237.
Amino acid biosynthesis in the halophilic archaeon Haloarcula hispanica.

573. Matthey, U., Kaim, G., Braun, D., Wüthrich, K. and Dimroth, P. (1999) Eur. J. Biochem. 261, 459–467.
NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles.

574. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (1999) J. Biomol. NMR 14, 85–88.
[¹³C]-constant-time [¹⁵N,¹H]-TROSY-HNCA for sequential assignments of large proteins.

575. Wüthrich, K., Billeter, M., Riek, R., Wider, G., Hornemann, S. and Glockshuber, R. (1999) in Peptide Science - Present and Future (Y. Shimonishi, ed.) pp. 330–334, Kluwer, Dordrecht.
Prion protein structure and pathology of transmissible spongiform encephalopathies (TSE).

576. Liu, A., Riek, R., Zahn, R., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1999) Biopolymers Peptide Sci. 51, 145–152.
Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy.

577. Wimmer, R., Herrmann, T., Solioz, M. and Wüthrich, K. (1999) J. Biol. Chem. 274, 22597–22603.
NMR structure and metal interactions of the CopZ copper chaperone.

578. Pervushin, K.V., Wider, G., Riek, R. and Wüthrich, K. (1999) Proc. Natl. Acad. Sci. USA 96, 9607–9612.
The 3D NOESY-[¹H,¹⁵N,¹H]-ZQ-TROSY NMR experiment with diagonal peak suppression.

579. Riek, R., Prêcheur, B., Wang, Y., Mackay, E.A., Wider, G., Güntert, P., Liu, A., Kägi J.H.R. and Wüthrich, K. (1999) J. Mol. Biol. 291, 417–428.
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.

580. Fernàndez, C., Szyperski, T., Billeter, M., Ono, A., Iwai, H., Kainosho, M. and Wüthrich, K. (1999) J. Mol. Biol. 292, 609–617.
Conformational changes of the BS2 operator DNA upon complex formation with the Antennapedia homeodomain studied by NMR with ¹³C/¹⁵N-labeled DNA.

581. Wider, G. und Wüthrich, K. (1999) Curr. Opin. Struct. Biol. 9, 594–601.
NMR spectroscopy of large molecules and multimolecular assemblies in solution.

582. Wüthrich, K. (1999) in Biological Physics, AIP Conf. Proc. 487, 3–7.
Hydration of proteins, nucleic acids and protein–DNA complexes in solution.

583. Szyperski, T., Fernandéz, C., Ono, A., Wüthrich, K. and Kainosho, M. (1999) J. Magn. Reson. 140, 491–494.
The 2D {³¹P} spin-echo-difference constant-time [¹³C,¹H]-HMQC experiment for simultaneous determination of ³J_H3’P and ³J_C4’P in ¹³C-labeled nucleic acids and their protein complexes.

584. Szyperski, T., Glaser, R.W., Hochuli, M., Fiaux, J., Sauer, U., Bailey, J.E. and Wüthrich, K. (1999) Metabolic Eng. 1, 189–197.
Bioreaction network topology and metabolic flux ratio analysis by biosynthetic fractional ¹³C labeling and two-dimensional NMR spectroscopy.

585. Sauer, U., Lasko, D.R., Fiaux, J., Hochuli, M., Glaser, R., Szyperski, T., Wüthrich, K. and Bailey, J.E. (1999) J. Bacteriol. 181, 6679–6688.
Metabolic Flux Ratio (METAFoR) analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism.

586. Salzmann, M., Wider, G., Pervushin, K. and Wüthrich, K. (1999) J. Biomol. NMR 15, 181– 184.
Improved sensitivity and coherence selection for [¹⁵N,¹H]-TROSY elements in triple resonance experiments.

587. Wüthrich, K. (1999) in Hydration Processes in Biology (M.C. Bellissent-Funel, ed.) pp. 251–258, IOS Press, Amsterdam.
NMR structure determination of biological macromolecules and studies of hydration in solution.

588. Zahn, R., Liu, A., Lührs, T., Riek, R., von Schroetter, C., López Garcia, F., Billeter, M., Calzolai, L., Wider, G. and Wüthrich, K. (2000) Proc. Natl. Acad. Sci. USA 97, 145–150.
NMR solution structure of the human prion protein.

589. Pervushin, K., Fernàndez, C., Riek, R., Ono, A. Kainosho, M. and Wüthrich, K. (2000) J. Biomol. NMR 16, 39–46.
Determination of ^h2J_NN and ^h1J_HN coupling constants across Watson–Crick base pairs in the Antennapedia homeodomain–DNA complex using TROSY.

590. Lòpez Garcia, F., Szyperski, T., Dyer, J.H., Choinowski, T., Seedorf, U., Hauser, H. and Wüthrich, K. (2000) J. Mol. Biol. 295, 595–603.
NMR structure of the sterol carrier protein-2: implications for the biological role.

591. Liu A., Riek, R., Wider, G., von Schroetter, C., Zahn, R. and Wüthrich, K. (2000) J. Biomol. NMR 16, 127–138.
NMR experiments for resonance assignments of ¹³C, ¹⁵N doubly-labeled flexible polypeptides: Application to the human prion protein hPrP(23–230).

592. Wüthrich, K. (2000) Nature Struct. Biol. 7, 188–189.
Protein recognition by NMR.

593. Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S. and Wüthrich, K. (2000) Protein Sci. 9, 1038–1041.
NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori.

594. Hochuli, M., Szyperski, T. and Wüthrich, K. (2000) J. Biomol. NMR 17, 33–42.
Deuterium isotope effects on the central carbon metabolism of Escherichia coli cells grown on a D₂O-containing minimal medium.

595. Wüthrich, K. (1999) in Kyoto Prizes & Inamori Grants 1998, pp. 104–141, The Inamori Foundation, Kyoto, Japan.
From Nature to Natural Science.

596. Lopez Garcia, F., Zahn, R., Riek, R. and Wüthrich, K. (2000) Proc. Natl. Acad. Sci. USA 97, 8334–8399.
NMR structure of the bovine prion protein.

597. Calzolai, L., Lysek, D.A., Güntert, P., von Schroetter, C., Riek, R., Zahn, R. and Wüthrich, K. (2000) Proc. Natl. Acad. Sci. USA 97, 8340–8345.
NMR structures of three single-residue variants of the human prion protein.

598. Pervushin, K., Braun, D., Fernàndez C. and Wüthrich, K. (2000) J. Biomol. NMR 17, 195– 202.
[¹⁵N,¹H]/[¹³C,¹H]-TROSY for simultaneous detection of backbone ¹⁵N–¹H, aromatic ¹³C– ¹H and side-chain ¹⁵N–¹H₂ correlations in large proteins.

599. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (2000) J. Am. Chem. Soc. 122, 7543–7548.
NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments.

600. Riek, R., Pervushin, K. and Wüthrich. K. (2000) Trends Biochem. Sci. 25, 462– 468.
TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.

601. Güntert, P., Salzmann, M., Braun, D. and Wüthrich, K. (2000) J. Biomol. NMR 18, 129 – 137.
Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER.

602. Billeter, M. and Wüthrich, K. (2000) Arch. Virol. (Suppl.) 16, 251 – 263.
The prion protein globular domain and disease-related mutants studied by molecular dynamics simulations.

603. Ellgaard, L., Riek, R., Braun, D., Herrmann, T., Helenius, A. and Wüthrich, K. (2001) FEBS Lett. 488, 69–73.
Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment.

604. Liu, A., Luginbühl, P., Zerbe, O., Ortenzi, C., Luporini, P. and Wüthrich, K. (2001) J. Biomol. NMR 19, 75 – 78.
NMR structure of the pheromone Er-22 from Euplotes raikovi.

605. Horst, R., Damberger, F., Peng, G., Nikonova, L., Leal, W.S. and Wüthrich, K. (2001) J. Biomol. NMR 19, 79 – 80.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.

606. Riek, R., Pervushin, K., Fernàndez, C., Kainosho, M. and Wüthrich, K. (2001) J. Am. Chem. Soc. 123, 658–664.
[¹³C, ¹³C]- and [¹³C, ¹H]-TROSY in a triple resonance experiment for ribose–base and intrabase correlations in nucleic acids.

607. Frey, A.D., Fiaux, J., Szypersky, T., Wüthrich, K., Bailey, J.E. and Kallio, P.T. (2001) Appl. Environm. Microbiol. 67, 680 – 687.
Dissection of central carbon metabolism of hemoglobin-expressing Escherichia coli by ¹³C nuclear magnetic resonance flux distribution analysis in microaerobic bioprocesses.

608. Fernandéz, C., Adeishvili, K. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 2358– 2363.
Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.

609. Ellgaard, L., Riek, R., Herrmann, T., Güntert, P., Braun, D., Helenius, A. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 3133–3138.
NMR structure of the calreticulin P-domain.

610. Wüthrich, K. (2001) in Prionen und Prionenkrankheiten (B. Hörnlimann, D. Riesner und H. Kretschmar, Hrsg.) pp. 69–-73, de Gruyter, Berlin.
Die Bestimmung der dreidimensionalen Struktur des zellulären Prion-Proteins PrP^C.

611. Wüthrich, K. and Riek, R. (2001) Adv. Protein Chem. 57, 55–82.
Three-dimensional structures of prion proteins.

612. Wüthrich, K. (2001) in International Tables for Crystallography, Vol. F: Crystallography of Biological Macromolecules (M.G. Rossmann and E. Arnold, eds.) pp. 464–467, Kluwer, Dordrecht, The Netherlands.
Nuclear magnetic resonance (NMR) spectroscopy.

613. Güntert, P. and Wüthrich, K. (2001) Comp. Phys. Commun. 138, 155–169.
Sampling of conformation space in torsion angle dynamics calculations.

614. Fernández, C., Hilty, C., Bonjour, S., Adeishvili, K., Pervushin, K. and Wüthrich, K. (2001) FEBS Lett. 504, 173–178.
Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.

615. Wüthrich, K. (2001) in Encyclopedia of Life Sciences, online at www.els.net.
Nuclear magnetic resonance (NMR) spectroscopy of proteins.

616. Wüthrich, K. (2001) Nature Struct. Biol. 8, 923–925.
The way to NMR structures of proteins.

617. Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 14374–14379.
NMR structure reveals intramolecular regulation mechanism for pheromone binding and release.

618. Riek, R., Güntert, P., Döbeli, H., Wipf, B. and Wüthrich, K. (2001) Eur. J. Biochem. 268, 5930–5936.
NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Ab(1-40)^ox and Ab(1-42)^ox.

619. Zahn, R., Damberger, F., Ortenzi, C., Luporini, P. and Wüthrich, K. (2001) J. Mol. Biol. 313, 923–931.
NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds.

620. Di Giuseppe, G., Miceli, C., Zahn, R., Damberger, F., Wüthrich, K. and Luporini, P. (2002) J.Eukaryot. Microbiol. 49, 86–92.
A structurally deviant member of the Euplotes raikovi pheromone family: Er-23.

621. Emmerling, M., Dauner, M., Ponti, A., Fiaux, J., Hochuli, M., Szyperski, T., Wüthrich, K., Bailey, J.E. and Sauer, U. (2002) J. Bacteriol. 184, 152–164.
Metabolic flux responses to pyruvate kinase knockout in Escherichia coli.

622. Pellecchia, M., Sem, D. S. and Wüthrich, K. (2002) Nature Rev. Drug Disc. 1, 211–219.
NMR in drug discovery.

623. Frickel, E.M., Riek, R., Jelesarov, I., Helenius, A., Wüthrich, K. and Ellgaard, L. (2002) Proc. Natl. Acad. Sci. USA 99, 1954–1959.
TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

624. Dauner, M., Sonderegger, M., Hochuli, M., Szyperski, T., Wüthrich, K., Hohmann, H.P., Sauer, U. and Bailey, J.E. (2002) Appl. Env. Microbiol. 68,1760–1771.
Intracellular carbon fluxes in riboflavin-producing Bacillus subtilis during growth on two-carbon substrate mixtures.

625. Luginbühl, P. and Wüthrich, K. (2002) Progr. Nucl. Magn. Reson. Spect. 40, 199–247.
Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules.

626. Herrmann, T., Güntert, P. and Wüthrich, K. (2002) J. Mol. Biol. 319, 209–227.
Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.

627. Etezady-Esfarjani, T., Hilty, C., Wüthrich, K., Rueping, M., Schreiber, J. and Seebach, D. (2002) Helv. Chim. Acta. 85, 1197–1209.
NMR-structural investigations of a β3-dodecapeptide with proteinogenic side chains in methanol and in aqueous solutions.

628. Fiaux, J., Bertelsen, E., Horwich, A. and Wüthrich, K. (2002) Nature 418, 207–211.
NMR analysis of a 900K GroEL–GroES complex.

629. Wüthrich, K. and Wider, G. (2002) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.), Vol. 9, pp. 468–477, Wiley, New York.
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.

630. Ellgaard, L., Bettendorff, P., Braun, D., Herrmann, T., Fiorito, F., Jelesarov, I., Güntert, P., Helenius, A. and Wüthrich, K. (2002) J. Mol. Biol. 322, 773–784.
NMR structures of 36- and 73-residue fragments of the calreticulin P-domain.

631. Hilty, C., Fernández, C., Wider, G. and Wüthrich, K. (2002) J. Biomol. NMR 23, 289–301.
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.

632. Riek, R., Fiaux, J., Bertelsen, E., Horwich, A. and Wüthrich, K. (2002) J. Am. Chem. Soc. 124, 12144–12153.
Solution NMR techniques for large molecular and supramolecular structures.

633. Fernández, C., Hilty, C., Wider, G. and Wüthrich, K. (2002) Proc. Natl. Acad. Sci. USA 99, 13533–13537.
Lipid–protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.

634. Lee, D., Damberger, F., Guihong, P., Horst, R., Güntert, P., Nikonova, L., Leal, W. and Wüthrich, K. (2002) FEBS Lett. 531, 314–318.
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.

635. Herrmann, T., Güntert, P. and Wüthrich, K. (2002) J. Biomol. NMR 24, 171–189. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS.

636. Fiaux, J., Cakar, Z.P., Sonderegger, M., Wüthrich, K., Szyperski, T. and Sauer, U. (2003) Eukaryotic Cell 2, 170–180.
Metabolic-flux profiling of the yeasts Saccharomyces cerevisiae and Pichia stipitis.

637. Etezady-Esfarjani, T., Peti, W. and Wüthrich, K. (2003) J. Biomol. NMR 25, 167–168.
NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima.

638. Zahn, R., Güntert, P., von Schroetter, C. and Wüthrich, K. (2003) J. Mol. Biol. 326, 225–234.
NMR structure of a variant human prion protein with two disulfide bridges.

639. Lührs, T., Riek, R., Güntert, P. and Wüthrich, K. (2003) J. Mol. Biol. 326, 1549–1557.
NMR structure of the human doppel protein.

640. Wüthrich, K. (2003) Angew.Chem. Int. Ed. 42, 3340−3363.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

641. Wüthrich, K. (2003) Angew.Chem. 115, 3462−3486.
NMR–Untersuchungen von Struktur und Funktion biologischer Makromoleküle (Nobel-Vortrag).

642. Wüthrich, K. (2003) J. Biomol. NMR 27, 1–12.
Kurt Wüthrich: Biographical note.

643. Wüthrich, K. (2003) J. Biomol. NMR 27, 13–39.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

644. Wüthrich, K. (2003) in Les Prix Nobel 2002 (T. Frängsmyr and B. Lundeberg, eds.)
Almquist and Wiksell International, Stockholm, Sweden, pp. 219–234.

645. Wüthrich, K. (2003) in Les Prix Nobel 2002 (T. Frängsmyr and B. Lundeberg, eds.)
Almquist and Wiksell International, Stockholm, Sweden, pp. 235–267. NMR studies of structure and function of biological macromolecules (Nobel Lecture).

646. Hochuli, M., Wüthrich, K. and Steinmann, B. (2003) NMR Biomed. 16, 224–236.
Two-dimensional NMR spectroscopy of urinary glycosaminoglycans from patients with different mucopolysaccharidoses.

647. Hiller, S., Kohl, A., Fiorito, F., Herrmann, T., Wider, G., Tschopp, J., Grütter, M. and
Wüthrich, K. (2003) Structure 11, 1198–1205. NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain.

648. Braun, D., Wüthrich, K. and Wider, G. (2003) J. Magn. Reson. 165, 89–94.
Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.

649. Hilty, C., Wider, G., Fernández, C. and Wüthrich, K. (2003) J. Biomol. NMR 27, 377–382.
Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles.

650. Fernández, C. and Wüthrich, K. (2003) FEBS Lett. 555, 144–150.
NMR solution structure determination of membrane proteins reconstituted in detergent micelles.

651. Wüthrich, K. (2003) Biosci. Reports 23, 119−168.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).

652. Wüthrich, K. and Wider, G. (2003) Magn. Reson. Chem. 41, 580-588.
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.

653. Etezady-Esfarjani, T. and Wüthrich, K. (2004) J. Biomol. NMR 29, 99–100.
NMR assignment of TM1442, a putative anti-σ factor antagonist from Thermotoga maritima.

654. Fernández, C., Hilty, C., Wider, G., Güntert, P. and Wüthrich, K. (2004) J. Mol. Biol. 336, 1211–1221.
NMR structure of the integral membrane protein OmpX.

655. Tafer, H., Hiller, S., Hilty, H., Fernández, C. and Wüthrich, K. (2004) Biochemistry 43, 860–869.
Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX).

656. Hilty, C., Wider, G., Fernández, C. and Wüthrich, K. (2004) Chem BioChem 5, 467–473.
Membrane protein – lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.

657. Fiaux, J., Bertelsen, E.B., Horwich, A.L. and Wüthrich, K. (2004) J. Biomol. NMR 29, 280–297.
Uniform and residue-specific ¹⁵N-labeling of proteins on a highly deuterated background.

658. Iwai, H., Wider, G and Wüthrich, K. (2004) J. Biomol. NMR 29, 395–398.
NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups

659. Etezady-Esfarjani, T., Herrmann, T., Peti, W., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J. Biomol. NMR 29, 403–406.
NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis.

660. Almeida, M.S., Peti, W. and Wüthrich, K. (2004) J. Biomol. NMR 29, 453–454.
¹H-, ¹³C- and ¹⁵N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima.

661. Peti, W., Etezady-Esfarjani, T., Herrmann, T., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J. Struct. Funct. Genom. 5, 205–215.
NMR for structural proteomics of Thermotoga maritima: screening and structure determination.

662. Lysek, D.A. and Wüthrich, K. (2004) Biochemistry 43, 10393–10399.
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

663. Lysek, D.A., Nivon, L.G. and Wüthrich, K. (2004) Gene 341, 249–253.
Amino acid sequence of the Felis catus prion protein.

664. Hornemann, S., Schorn, C. and Wüthrich, K. (2004) EMBO Reports 5, 1159–1164.
NMR structure of the bovine prion protein isolated from healthy calf brains.

665. Kelker, M.S., Foss, T.R., Peti, W., Teyton, L., Kelly, J.W., Wüthrich, K. and Wilson, I.A. (2004) J. Mol. Biol. 342, 1237–1248.
Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 Ǻ.

666. Pervushin, K., Wider, G., Iwai, H. and Wüthrich, K. (2004) Biochemistry 43, 13937–13943.
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.

667. Lysek, D.A., Schorn, C., Nivon, L.G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 640–645.
Prion protein NMR structures of cats, dogs, pigs and sheep.

668. Gossert, A.D., Bonjour, S., Lysek, D.A., Fiorito, F. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 646–650.
Prion protein NMR structures of elk and mouse/elk hybrids.

669. Calzolai, L., Lysek, D.A., Pérez, D.R., Güntert, P. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 651–655.
Prion protein NMR structures of chickens, turtles, and frogs.

670. Page, R., Peti, W., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 1901–1905.
NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.

671. Michel, E., Damberger, F.F., Chen, A.M., Ishida, Y., Leal, W.S. and Wüthrich, K. (2005) J. Biomol. NMR 31, 65.
Assignments for the Bombyx mori pheromone-binding protein fragment BmPBP (1–128) at pH 6.5.

672. Pérez, D.R. and Wüthrich, K. (2005) J. Biomol. NMR 31, 260.
NMR assignment of the Xenopus laevis prion protein fragment xlPrP(98–226).

673. Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorf, P., Jelesarov, I., Grütter, M.G., Wüthrich, K., Glockshuber, R. and Capitani, G. (2005) EMBO J. 24, 2075–2086.
Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD.

674. Peti, W., Herrmann, T., Zagnitko, O., Grzechnik, S.K. and Wüthrich, K. (2005) Proteins 59, 387–390.
NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.

675. Columbus, L., Peti, W., Etezady-Esfarjani, T., Herrmann, T. and Wüthrich, K. (2005) Proteins 60, 552–557.
NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.

676. Hiller, S., Fiorito, F., Wüthrich, K. and Wider, G. (2005) Proc. Natl. Acad. Sci. USA 102, 10876–10881.
Automated projection spectroscopy (APSY).

677. Hiller, S., Wider, G., Etezady-Esfarjani, T., Horst, R. and Wüthrich, K. (2005) J. Biomol. NMR. 32: 61–70.
Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures.

678. Horst, R., Bertelsen, E.B., Fiaux, J., Wider, G., Horwich, A.L. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 12748–12753.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

679. Peti, W., Johnson, M.A., Herrmann, T., Neuman, B.W., Buchmeier, M.J., Nelson, M., Joseph, J., Page, R., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2005) J. Virol. 79, 12905– 12913.
Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.

680. Fadel, W., Bettendorff, P., Herrmann, T., de Zevedo Jr, W.F., Oliveira, E.B., Yamane, T. and Wüthrich, K. (2005) Toxicon, 46, 759–767.
Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus.

681. Almeida, M.S., Herrman, T., Peti, W., Wilson, I.A. and Wüthrich, K. (2005) Protein Sci. 14, 2880–2886.
NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: Implications for 216 homologous DUF59 proteins.

682. Lee, D., Hilty, C., Wider, G. and Wüthrich, K. (2006) J. Magn. Reson. 178, 72–76.
Effective rotational correlation times of proteins from NMR relaxation interference.

683. Baker, K.A., Hilty, C., Peti, W., Prince, A., Pfaffinger, P.J., Wider, G., Wüthrich, K. and Choe, S. (2006) Biochemistry 45, 1663–1672.
NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain.

684. Lührs, T., Zahn, R. and Wüthrich, K., (2006) J. Mol. Biol. 357, 833–841.
Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions.

685. Peti, W., Page, R., Moy, K., O’Neil-Johnson, M., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) J. Struct. Funct. Genom. 6, 259–267.
Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR.

686. Etezady-Esfarjani, T., Herrmann, T., Horst, R. and Wüthrich, K. (2006) J. Biomol. NMR. 34, 3–11.
Automated protein NMR structure determination in crude cell-extract.

687. Johnson, M., Peti, W., Herrmann, T., Wilson, I. and Wüthrich, K. (2006) Protein Sci. 15, 1030–1041.
Solution structure of As11650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.

688. Serrano, P., Almeida, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 45.
NMR assignment of the protein nsp3a from SARS-CoV.

689. Almeida, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 46.
NMR assignment of the SARS-CoV protein nsp1.

690. Fiorito, F., Hiller, S., Wider, G. and Wüthrich, K. (2006) J. Biomol. NMR 35, 27–37.
Automated resonance assignment of proteins: 6D APSY-NMR.

691. Etezady-Esfarjani, T., Placzek, W.J., Herrmann, T. and Wüthrich, K. (2006) Magn. Reson. Chem. 44, S61–S70.
Solution structures of the putative anti-σ-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.

692. Horst, R., Wider, G., Fiaux, J., Bertelsen, E.B., Horwich, A.L. and Wüthrich, K. (2006) Proc. Natl. Acad. Sci. USA 103, 15445–15450.
Proton–proton Overhauser NMR spectroscopy with polypeptide chains in large structures.

693. Placzek, W.J., Almeida, M.A. and Wüthrich, K. (2006) J. Biomol. NMR 36, 59.
NMR assignment of a human cancer-related nucleoside triphosphatase.

694. Banci, L., Bertini, I., Cantini, F., DellaMalva, N., Herrmann, T., Rosato, A. and Wüthrich, K. (2006) J. Biol. Chem. 281, 29141–29147.
Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein.

695. Placzek, W.J., Almeida, M.S. and Wüthrich, K. (2007) J. Mol. Biol. 367, 788–801.
NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase.

696. Almeida, M.S., Johnson, M.A., Herrmann, T., Geralt, M. and Wüthrich, K. (2007) J.Virol. 81, 3151–3161.
Novel β-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.

697. Gossert, A.D., Hiller, S., Fiorito, F. and Wüthrich K. (2007) J. Biomol. NMR 38, 195.
NMR assignment of the E. coli type 1 pilus protein FimF.

698. Johnson, M.A., Southworth, M.W., Perler, F.B. and Wüthrich K. (2007) Biomol. NMR Assign. 1, 19–21.
NMR assignment of a KlbA intein precursor from Methanococcus jannaschii.

699. Placzek, W.J., Etezady-Esfarjani, T., Herrmann, T., Pedrini, B., Peti, W., Alimenti, C., Luporini, P. and Wüthrich, K. (2007) IUBMB Life 59, 578–585.
Cold-adapted signal proteins: NMR structures of pheromones from the antarctic ciliate Euplotes nobilii.

700. Johnson, M.A., Southworth, M.W., Herrmann, T., Brace, L., Perler, F.B. and Wüthrich, K. (2007) Protein Sci. 16, 1316–1328.
NMR structure of a Klba intein precursor from Methanococcus jannaschii.

701. Damberger, F.F., Ishida, Y., Leal, W.S. and Wüthrich, K. (2007) J. Mol. Biol. 373, 811–819.
Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5.

702 Serrano, P., Johnson, M.A., Almeida, M.S., Horst, R., Herrmann, T., Joseph, J.S., Neuman, B.W., Subramanian V., Saikatendu, K.S., Buchmeier, M.J., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2007) J.Virol. 81, 12049–12060.
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.

703. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B. and Wüthrich, K. (2007) Biomol. NMR Assign. 1, 191–194.
NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3.

704. Etezady-Esfarjani, T., Hiller, S., Villalba, C. and Wüthrich, K. (2007) J. Biomol. NMR 39, 229–238.
Cell-free protein synthesis of perdeuterated proteins for NMR studies.

705. Hiller, S., Wasmer, C., Wider, G. and Wüthrich, K. (2007) J. Am. Chem. Soc. 129, 10823–10828.
Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy.

706. Sigurdson, C.J., Nilsson, K.P.R., Hornemann, S., Manco, G., Polymenidou, M., Schwarz, P., Leclerc, M., Hammarström, P., Wüthrich, K. and Aguzzi, A. (2007) Nature Methods 12, 1023–1030.
Prion strain discrimination using luminescent conjugated polymers.

707. Horst, R., Fenton, W.A., Englander, W.S., Wüthrich, K. and Horwich A.L. (2007) Proc. Natl. Acad. Sci. USA 104, 20788–20792.
Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution.

708. Pedrini, B., Placzek, W.J., Koculi, E., Alimenti, C., LaTerza, A., Luporini, P. and Wüthrich, K. (2007) J. Mol. Biol. 372, 277–286.
Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from the antarctic ciliate Euplotes nobilii.

709. Gossert, A.D., Bettendorff, P., Puorger, C., Vetsch, M., Herrmann, T., Glockshuber, R. and Wüthrich, K. (2008) J. Mol. Biol. 375, 752–763.
NMR structure of the Escherichia coli type 1 pilus subunit FimF and its interactions with other pilus subunits.

710. Christen, B., Wüthrich, K. and Hornemann, S. (2008) FEBS J. 275, 263–270.
Putative prion protein from Fugu (Takifugu rubripes).

711. Hiller, S., Wider, G., Imbach, L.L. and Wüthrich, K. (2008) Angew. Chem. Int. Ed. 47, 977–981.
Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX.

712. Zhang, Q., Horst, R., Geralt, M., Ma, X., Hong, W., Finn, M.G. Stevens, R. and Wüthrich, K. (2008) J. Am. Chem. Soc. 130, 7357–7363.
Microscale NMR screening of new detergents for membrane protein structural biology.

713. Neuman, B.W., Joseph, J.S., Saikatendu, K.S., Serrano, P., Chatterjee, A., Johnson, M.A., Liao, L., Klaus, J.P., Yates, J.R., Wüthrich, K., Stevens, R., Buchmeier, M.J. and Kuhn, P. (2008) J.Virol. 82, 5279–5294.
Proteomics analysis unravels the functional repertoire of Coronavirus nonstructural protein 3.

714. Volk, J., Herrmann, T. and Wüthrich, K. (2008) J. Biomol. NMR 41, 127–138.
Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH.

715. Christen, B., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2008) J. Mol. Biol. 383,306–312.
NMR structure of the bank vole prion protein at 20 ^◦C contains a structured loop of residues 165–171.

716. Billeter, M., Wagner, G. and Wüthrich K. (2008) J. Biomol. NMR 42, 155–158.
Solution NMR structure determination of proteins revisited.

717. Fiorito, F., Herrmann, T., Damberger, F.F. and Wüthrich K. (2008) J. Biomol. NMR 42, 23–33.
Automated amino acid side-chain NMR assignment of proteins using ¹³C- and ¹⁵N-resolved 3D [¹H,¹H]-NOESY.

718. Serrano, P., Johnson, M.A., Chatterjee, A., Pedrini, B. and Wüthrich, K. (2008) Biomol. NMR Assign. 2, 135–138.
NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV.

719. Hiller, S., Wider, G. and Wüthrich, K. (2008) J. Biomol. NMR. 42, 179–195.
APSY-NMR with proteins: practical aspects and backbone assignment.

720. Polymenidou, M., Moos, R., Scott, M., Sigurdson, C., Shi, Y.-Z, Yajima, B., Hafner-Bratkovic, I., Jerala, R., Hornemann, S., Wüthrich, K., Bellon, A., Vey, M., Garen, G., James, M.N.G., Kav, N. and Aguzzi, A. (2008) PLoS ONE 3, e3872, 1–17.
The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

721. Sigurdson, C.J., Nilsson, K.P., Hornemann, S., Heikenwalder, M., Manco, G., Schwarz, P., Ott, D., Rülicke, T., Liberski, P.P., Julius, C., Falsig, J., Stitz, L., Wüthrich, K. and Aguzzi, A. (2009) Proc. Natl. Acad. Sci. USA 106, 304–309.
De novo generation of transmissible spongiform encephalopathy by mouse transgenesis.

722. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B., Joseph, J.J., Neuman, B.W., Saikatendu, K., Buchmeier, M.J., Kuhn, P. and Wüthrich, K. (2009) J. Virol. 83, 1823–1836
NMR structure shows that the SARS-unique domain contains a macrodomain fold.

723. Hornemann, S., Christen, B., von Schroetter, C., Pérez, D. and Wüthrich, K. (2009) FEBS J. 276, 2359–2367.
Prion protein library of recombinant constructs for structural biology.

724. Christen, B., Hornemann, S., Damberger, F. F. and Wüthrich, K. (2009) J. Mol. Biol. 389, 833–845.
Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the β2–α2 loop is modulated by long-range sequence effects.

725. Alimenti,C., Vallesi, A., Pedrini, B., Wüthrich, K. and Luporini, P. (2009) IUBMB Life 61, 838–845.
Molecular cold-adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes.

726. Honnappa, S., Montenegro Gouveia, S., Weisbrich, A., Damberger, F.F., Bhavesh, N.S., Jawhari, H., Grigoriev, I., van Rijssel, F.J.A., Buey, R.M., Lawera, A., Jelesarov, I., Winkler, F.K., Wüthrich, K, Akhmanova, A. and Steinmetz, M.O (2009) Cell 138, 366–376.
An EB1-binding motif acts as a microtubule tip localization signal.

727. Hornemann, S., von Schroetter, C., Damberger, F.F. and Wüthrich, K. (2009) J. Biol. Chem. 284, 22713–22721.
Prion protein–detergent micelle interactions studied by NMR in solution.

728. Serrano, P., Johnson, M.A., Chatterjee, A., Neuman, B.W., Joseph, J.S., Buchmeier, M.J., Kuhn, P. and Wüthrich, K. (2009) J. Virol. 83, 12998–13008.
Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3.

729. Stanczak, P., Horst, R., Serrano, P. and Wüthrich, K. (2009) J. Am. Chem. Soc. 131, 18450–18456
NMR characterization of membrane protein–detergent micelle solutions by use of microcoil equipment.

730. De Groot, C.O., Jelesarov, I., Damberger, F.F., Bjelić, S., Schärer, M.A., Bhavesh, N.S., Grigoriev, I., Buey, R.M., Wüthrich, K., Capitani, G., Akhmanova, A. and Steinmetz, M.O. (2010) J. Biol. Chem. 285, 5802–5814.
Molecular insights into mammalian end-binding protein heterodimerization.

731. Pérez, D.R., Damberger, F.F. and Wüthrich, K. (2010) J. Mol. Biol. 400, 121–128; 402, 929–930.
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.

732. Sigurdson, C.J., Nilsson, K.P.R., Hornemann, S., Manco, G., Fernández-Borges, Schwarz, P., Wüthrich, K. and Aguzzi, A. (2010) J. Clin. Invest. 120, 2590–2599.
A molecular switch controls interspecies prion disease transmission in mice.

733. Johnson, M.A., Chatterjee, A., Neuman, B.W. and Wüthrich, K. (2010) J. Mol. Biol. 400, 724–742.
SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.

734. Vallesi, A., Alimenti, C., Di Giuseppe, G., Dini, F., Pedrini, B., Wüthrich, K. and Luporini, P. (2010) Polar Science 4, 237–244.
The water-born protein pheromones of the polar protozoan ciliate, Euplotes nobilii: Coding genes and molecular structures.

735. Johnson, M.A., Jaudzems, K. and Wüthrich, K. (2010) J. Mol. Biol. 402, 619–628.
NMR structure of the SARS-CoV nonstructural protein 7 in solution at pH 6.5.

736. Vila, J.A., Serrano, P., Wüthrich, K. and Scheraga, H.A. (2010) J. Biomol. NMR 48, 23–30.
Sequential nearest-neighbor effects on computed ¹³C^α chemical shifts.

737. Elsliger, M-A., Deacon, A.M., Godzik, A., Lesley, S.A., Wooley, J., Wüthrich, K. and Wilson, I.A. (2010) Acta Cryst. F. 66, 1137–1142.
The JCSG high-throughput structural biology pipeline.

738. Wüthrich, K. (2010) Acta Cryst. F 66, 1365–1366.
NMR in a crystallography-based high-throughput protein structure-determination environment.

739. Jaudzems, K., Geralt, M., Serrano, P., Mohanty, B., Horst, R., Pedrini, B., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F 66, 1367–1380.
NMR structure of the protein NP_247299.1: comparison with the crystal structure.

740. Mohanty, B., Serrano, P., Pedrini, B., Jaudzems, K., Geralt, M., Horst, R., Herrmann, T., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F 66, 1381–1392.
Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.

741. Serrano, P., Pedrini, B., Geralt, M., Jaudzems, K., Mohanty, B., Horst, R., Herrmann, T., Elsliger, M-A., Wilson, I.A. and Wüthrich, K. (2010) Acta Cryst. F 66, 1393–1405.
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.

742. Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K. and van Gunsteren, W.F. (2011) Eur Biophys. J. 40, 39–58.
Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle.

743. Orcajo-Rincón, A.L., Ortega-Gutiérrez, S., Serrano, P., Torrecillas, I.R., Wüthrich, K., Campillo, M., Pardo, L.,Viso, A., Benhamú, B. and López-Rodriguez, M.L. (2011) J. Med. Chem. 54, 1096–1100.
Development of non-peptide ligands of growth factor receptor-bound protein 2-Src homology 2 domain using molecular modeling and NMR spectroscopy.

744. Di Giuseppe, G., Erra, F., Dini, F., Alimenti, C., Vallesi, A., Pedrini, B., Wüthrich, K. and Luporini, P. (2011). Proc. Natl. Acad. Sci. USA. 108, 3181–3186.
Antarctic and Arctic populations of the ciliate Euplotes nobilii show common pheromone-mediated cell-cell signaling and cross-mating.

745. Michel, E., Damberger, F.F., Ishida, Y., Fiorito, F., Lee, D.H., Leal, W.S. and Wüthrich, K. (2011) J. Mol. Biol. 408, 922–931.
Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein.

746. Wahab, A.T., Serrano, P., Geralt, M. and Wüthrich, K. (2011) Protein Science 20, 1137–1144.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.

747. Koculi, Eda, Horst, R., Horwich, A.L. and Wüthrich, K. (2011) Protein Science 20, 1380–1386.
Nuclear Magnetic Resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.

748. Horst, R., Horwich, A.L. and Wüthrich, K. (2011) J. Am. Chem. Soc. 20, 16354–16357.
Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR.

749. Damberger, F.F., Christen, B., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2011) Proc. Natl. Acad. Sci. USA 108, 17308–17313.
Cellular prion protein conformation and function.

750. Sigurdson, C.J., Joshi-Barr, S., Bett, C., Winson, O., Manco, G., Schwarz, P., Rülicke, T., Nilsson, K.P.R., Margalith, I., Raeber, A., Peretz, D., Hornemann, S., Wüthrich, K. and Aguzzi, A. (2011) J. Neurosci. 31, 13840–13847.
Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.

751. Liu, J.J, Horst, R., Katritch, V., Stevens, R.C. and Wüthrich, K. (2012) Science 335. 1106-1110.
Biased signaling pathways in β₂andreergic receptor characterized by ¹⁹F-NMR.

752. Horst, R., Stanczak, P., Serrano, P. and Wüthrich, K. (2012) J. Phys. Chem. B 116, 6775–6780..
Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solublized membrane protein OmpX.

753. Vallesi, A., Alimenti, C., Pedrini, B., Di Giuseppe, G., Dini, F., Wüthrich, K. and Luporini, P. (2012) Marine Genomics doi: 10.1016/j.margen.2012.03.004.
Coding genes and molecular structures of the diffusible signaling proteins (pheromones) of the polar ciliate, Euplotes nobilii.

754. Michel, E. and Wüthrich, K. (2012) J. Biomol. NMR 53, 43–51.
High-yield Escherichia coli-based cell-free expression of human protein. 

755. Serrano, P., Pedrini, B., Mohanty, B., Geralt, M., Herrmann, T. and Wüthrich K. (2012) J. Biomol.  NMR 53, 341–354.
The J-UNIO protocol for automated protein structure determination by NMR in solution.

756. Michel, E. and Wüthrich, K. (2012) FEBS. J. 279, 3176–3184.
Cell-free expression of disulfide-containing eukaryotic proteins for structural biology.

757. Stanczak, P., Zhang, Q., Horst, R., Serrano, P. and Wüthrich, K. (2012) J. Biomol. NMR 54, 129–133.
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles.

758. Christen, B., Hornemann, S., Damberger, F.F. and Wüthrich, K. (2012) J. Mol. Biol. 423, 796–502.
Prion protein mPrP[F175A]: Structure and stability in solution.

759. Horst, R., Stanczak, P., Stevens, R.C. and Wüthrich, K. (2012)  Angew. Chem. DOI: 10.1002/anie.201205474.
β₂-adrenergic receptor solutions for structural biology analyzed with micro-scale NMR diffusion measurements.

760.  Stevens, R., Cherezov, V., Katritch, V., Abagyan, R., Kuhn, P., Rosen, H. and Wüthrich, K. (2013) Nature Rev. Drug Discovery 12, 1–10.
The GPCR Network: a large-scale collaboration to determine human GPCR structure and function.

761.  Geralt, M., Alimenti, C., Vallesi, A., Luporini, P. and Wüthrich, K. (2013) Biology 2, 142–150.
Thermodynamic stability of psychrophilic and mesophilic pheromones of the protozoan ciliate Europlotes.

762.  Michel, E., Srisovska, L., Wüthrich, K. and Allain, F.H.-T. (2013) ChemBioChem 14, 457–466.
Amino acid-selective segmental isotope labeling of multidomain proteins for structural biology.

763.  Christen, B., Damberger, F.F., Pérez, D.R., Hornemann, S. and Wüthrich, K. (2013) Proc. Natl. Acad. Sci. USA 110, 8549–8554. Structural plasticity of the cellular prion protein and implications in health and disease.    

764.  Serrano, P., Geralt, M., Mohanty, B. and Wüthrich, K. (2013) Protein Science 22, 1000–1007.Structural representative of the protein family PF14466 has a new fold and establishes links with the C2 and PLAT domains from the widely distant Pfams PF00168 and PF01477.       

765.  Zarco-Zavala, M., Morales-Ríos, E., Serrano-Navarro, P., Wüthrich, K., Mendoza-Hernández, G., Ramírez-Silva L. and García-Trejo, J.J. (2013) Biochim. Biophys.  Acta 1827, 60. Corrigendum to “The ζ subunit of the α-proteobacterial F₁F_O-ATP synthase in Paracoccus denitrificans: A novel control mechanism of the central rotor” [Biochim. Biophys. Acta 1817S (2012) S27–S28].

766.  Didenko, T., Liu, J.J., Horst, R., Stevens, R.C. and Wüthrich, K. (2013) Curr. Opin. Struct. Biol. doi 10.1016/.sbi.2013.07.011.   Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.

767.  Pedrini, B., Serrano, P., Mohanty, B., Geralt, M. and Wüthrich, K. (2013) Biopolymers. doi 10.1002/bip.22348. NMR-profiles of protein solutions.

768.  Horst, R., Liu, J.J., Stevens, R.C. and Wüthrich, K. (2013) Angew. Chem. Int.Ed. doi10.1002/anie.201305286. β2-adrenergic receptor activation by agonistis studied with 19F-NMR.

769. Damberger, F.F., Michel, E., Ishida, Y., Leal, W.S. and Wüthrich, K. (2013) Proc. Natl. Acad. Sci. USA 110, 18680–18685. Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein.

770. Kurt, T.D., Bett, C., Fernández-Borges, N., Johi-Barr, S., Hornemann, S., Rülicke, T., Castilla, J., Wüthrich, K., Aguzzi, A. and Sigurdson, C.J. (2014) J. Neurosci. 34, 1022–1027. Prion transmission prevented by modifying the β2-α2 loop structure of host PrP^C.

771.  Sušac, L., Horst, R. and Wüthrich, K. (2014) ChemBioChem 15, 995–1000.
Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles.

772.  Horst, R., Stanczak, P. and Wüthrich, K. (2014) Structure 22, 1–6.
NMR polypeptide backbone conformation of the E. coli outer membrane protein W.

773.  Serrano, P., Geralt, M., Mohanty, B. and Wüthrich, K. (2014) J. Mol. Biol. 426, 2547–2553.
NMR structures of  -proteobacterial ATPase-regulating ζ-subunits.

774.  Wüthrich, K., Wilson I.A., Hilvert, D., Wolan, D. and De Wit, A., eds.  (2014) New Chemistry and New Opportunities from the Expanding Protein Universe.  Proceedings of the 23^rd Solvay Conference on Chemistry, World Scientific, Singapore.

775.  Wüthrich, K. (2014) New Chemistry and New Opportunities from the Expanding Protein Universe. Proceedings of the 23^rd Solvay Conference on Chemistry (Wüthrich, K., Wilson I.A., Hilvert, D. , Wolan, D. and De Wit, A., eds.), World Scientific, Singapore.Studies of GPCR conformations in non-crystalline milieus.

776.  Mohanty, B., Serrano, P., Geralt, M. and Wüthrich, K. (2014) J. Biomol. NMR 61, 83–87. NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042.

777.  Jaudzems, K., Pedrini, B., Geralt, M., Serrano, P. and Wüthrich, K. (2014) J. Biomol. NMR 61, 65–72. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumonia TIGR4.

778.  Dutta, S.K., Serrano, P., Proudfoot, A., Geralt, M., Pedrini, B., Herrmann, T. and Wüthrich, K. (2014) J. Biomol. NMR 61, 47–53.  APSY-NMR for protein backbone assignment in high-throughput structural biology.

779.  Horst. R. and Wüthrich, K. (2015) Bio-protocol 5 (14) http://www.bio-protocol.org/e1539. Micro-scale NMR experiments for monitoring the optimization of membrane protein solutions for structural biology.

780. Didenko, T., Proudfoot, A., Dutta, S.M., Serrano, P. and Wüthrich, K. (2015) Chem. Eur. J. 21, 1236–1239.  Non-uniform sampling and J-UNIO Automation for efficient protein NMR structure determination.

781.  Dutta, S.K., Serrano, P., Geralt, M., Axelrod, H.L., Xu, Q., Lesley, S.A., Godzik, A., Deacon, A.M., Elsliger, M.A., Wilson, I.A. and Wüthrich, K. (2015) Protein Sci. DOI: 10.1002/pro.2743. Cofactor-induced reversible folding of flavodoxin-4 from Lactobacillus acidophilus.

782. O’Connor, C., White, K.L., Doncescu, N., Didenko, T., Roth, B.L., Czaplicki, G., Stevens, R.C., Wüthrich, K. and Milon, A. (2015) Proc. Natl. Acad. Sci. USA 112, 11852–11857. NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opiod receptor.

783.  Lamichhane, R., Liu, J.J., Pljevaljcic, G., White, K.L., van der Schans, E., Katritch, V., Stevens, R.C., Wüthrich, K. and Millar, D.P. (2015) Proc. Natl. Acad. Sci. USA 112, 14254–14259. Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β₂AR.

784.  Wüthrich, K. (2015). JOSHA – J. Science, Humanities and Arts. DOI: 10.17160/josha.2.7.84. The NMR view of proteins.

785.  Sušac, L., O’Connor, C.O., Stevens, R.C. and Wüthrich, K. (2015) Angew. Chem. Int. Ed. 54, 15246–15249. In-membrane chemical modification (IMCM) for site-specific chromophore labeling of GPCRs.

786.  Martin, B.T., Serrano, P., Geralt, M. and Wüthrich K. (2016) Structure 24, 1–7. Nuclear magnetic resonance structure of a novel globular domain in RBM10 containing OCRE, the octamer repeat sequence motif.

787. Stepanyuk, G.A., Serrano, P., Peralta, E., Farr, C.L., Axelrod, H.L., Geralt, M., Das, D., Chiu, H.J., Jaroszewski, L., Deacon, A.M., Lesley, S.A., Elsliger, M.A., Godzik, A., Wilson, I.A., Wüthrich, K., Salomon, D.R. and Williamson, J.R. (2016) Acta Cryst D. 72, 497–511.  UHM–ULM interactions in the RBM39–U2AF65 splicing-factor complex.

788. Proudfoot, A., Axelrod, H.L., Geralt, M., Fletterick, R.J., Yumoto, F., Deacon, A.M., Elsliger, M.A., Wilson, I.A., Wüthrich, K. and Serrano, P. (2016) J. Mol.Biol. 428, 1130–1141.  Dlx5 homeodomain: DNA complex: structure, binding and effect of mutations related to split hand and food malformation syndrome.

789. Mohanty, B., Geralt, M., Wüthrich, K. and Serrano, P. (2016) Protein Sci. 25, 917–925. NMR reveals structural rearrangements associated to substrate insertion in nucleotide-adding enzymes.

790. Liu, D. and Wüthrich, K. (2016) J. Biomol. NMR 65, 1–5. Ring current shifts in ¹⁹F-NMR of membrane proteins.

791. Proudfoot, A., Geralt, M., Elsliger, M.A., Wilson, I.A., Wüthrich, K. and Serrano, P. (2016) Structure 24, ……/doi: 10.1007/s10858-016-0022-4. Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding. 

792. Proudfoot, A., Axelrod, H.L., Geralt, M., Fletterick, R.J., Yumoto, F., Deacon, A.M., Elsliger, M.A., Wilson, I.A., Wüthrich, K. and Serrano, P. (2016) J. Mol.Biol. 27, 1130–1141. Dlx5 homedomain/DNA complex; Structure, binding and effect of mutations related to split-hand and foot malformation syndrome. 

793.  Serrano, P., Dutta, S.K., Proudfoot, A., Mohanty, B., Susac, L., Martin, B., Geralt, M., Jaroszewski, L., Godzik, A., Elsliger, M., Wilson, I.A. and Wüthrich, K. (2016) FEBS J. …–…/doi:10.1111/febs.13751. NMR in structural genomics to increase structural coverage of the protein universe.

 794.  Beuck, C., Williamson, J.R., Wüthrich, K. and Serrano, P. (2016) Protein Sci. 25, 1545–1550. The acidic domain is a unique structural feature of the splicing factor SYNCRIP.

 795.  Landreh, M., Sawaya, M.R., Hipp, M.S., Eisenberg, D.S., Wüthrich, K. and Hartl, F.U. (2016) J. Intern. Med. 280, 164–176. The formation, function and regulation of amyloids: insights from structural biology. 

796. Serrano, P., Aubol, B.E., Keshwani, M.M., Flori, S., Ma, C.T., Dutta, S.K., Geralt, M., Wüthrich, K. and Adams J.A. (2016) J. Mol.Biol. 428, 2430–2445. Directional phosphorylation and nuclear transport of the splicing factor SRSF1 is regulated by an RNA recognition motif.       

797.  Leske, H., Hornemann, S., Herrmann, U.S., Zhu, C., Dametto, P., Li, B., Laferriere, F., Polymenidou, M., Pelczar, P., Reimann, R.R., Schwarz, P., Rushing, E.J., Wüthrich, K. and Aguzzi, A. (2017) PLOS ONE doi:10.137/journal.pone.0170503. Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.

798. Hou, Y., Hu, W., Li, X., Skinner, J.J., Liu, D. and Wüthrich, K. (2017) J. Biomol. NMR 68, 1–6. Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by ¹⁹F-NMR observation of 4-fluorphenylalanine.

799. Caldarulo, E., Barducci, A., Wüthrich, K. and Parrinello, M. (2017) Proc. Natl. Acad. Sci. USA 114, 9617–9622. Prion protein β2–α2 loop conformational landscape.

800. Eddy, M.T., Lee, M.-Y., Gao, Z.-G., White, K.L., Didenko, T., Horst, R., Audet, M., Stanczak, P., McClary, K.M., Han, G.W., Jacobson, K.A., Stevens, R. and Wüthrich, K. (2018) Cell 172, 68–80. Allosteric coupling of drug binding and intracellular signaling in the A_2A adenosine receptor.

801. Serrano, P., Hammond, J.A., Geralt, M. and Wüthrich, K. (2018) Biochemistry 57, 1563–1567. Splicing site recognition by synergy of three domains in splicing factor RBM10. 

802. Eddy, M.T., Gao, Z.-G., Mannes, P., Patel, N. Jacobson, K.A., Katritch, V., Stevens, R.C. and Wüthrich, K. (2018) J. Am. Chem. Soc. 140, 8228–8235. Extrinsic tryptophans as NMR probes of allosteric coupling in membrane proteins: application to the A_2A adenosine receptor.

803. Wüthrich, K., Grubbs, R.H., Visart de Bocarmé, T. and De Wit, A., eds. (2018) Catalysis in Chemistry and Biology.  Proceedings of the 24th Solvay Conference on Chemistry, World Scientific, Singapore.

804. Wüthrich, K. (2018) in ‘Il cibo: salute, cultura, piacere e tormento’, Atti del Meeting “Le Due Culture”, IX edizione, O. Zecchino, G. Capasso, M. De Felice, G. Marino, C. Pisano, eds., Fondazione Biogem, Ariano Irpino, Italy. Basic Scientific Research and Daily Human Life.

805. Sušac, L., Eddy, M.T., Didenko, T., Stevens, R.C. and Wüthrich, K. (2019) Proc. Natl. Acad. Sci. USA 115, 12733–12738. A_2A adenosine receptor functional states characterized by ¹⁹F-NMR.

806. Aubol, B.E., Serrano, P., Fattet, L., Wüthrich, K. and Adams, J.A. (2018) J. Biol. Chem. 293, 16751–16760. Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.

807. Shimada, I., Ueda, T., Kofuku, Y., Eddy, M.T. and Wüthrich, K. (2019) Nat. Rev. Drug Disc. 18, 59–82. GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures.