NMR Comes of Age with Nobel Recognition
"Nuclear magnetic resonance (NMR) has long been in the shadow of crystallography,"
says Peter Wright, Cecil H. and Ida M. Green Investigator in Medical Research
and chair of the Department of Molecular Biology at The Scripps Research
Institute (TSRI).
The 2002 Nobel Prize in Chemistry should change that. It was awarded
to Kurt Wüthrich for "his development of nuclear magnetic resonance
spectroscopy for determining the three-dimensional structure of biological
macromolecules in solution."
Of the two primary methods for determining the three-dimensional structure
of biological macromolecules—x-ray crystallography and NMR—crystallography
is older by several decades. NMR exploded on the scene in the early 1980s
as a viable technique for biomolecular structure determination when Wüthrich
worked out the methodologies needed to solve the first protein structures
using NMR.
Around the same time that Wüthrich was beginning to solve his first
structures with the method, NMR was arriving at TSRI with Wright and Professor
H. Jane Dyson, who came to the institute in 1984. NMR has been a part
of the structural biology research at TSRI ever since.
"The NMR group here is incredibly strong," says Wright. "And we have
one of the biggest and best-equipped NMR facilities in the world."
The principle NMR structural biologists at TSRI are:
H. Jane Dyson, who uses NMR to study the protein-folding process
and the nature and behavior of unfolded and partly folded forms of proteins,
including prion proteins and several newly-discovered, intrinsically unstructured
proteins.
Mirko Hennig, who develops new NMR methodology to study the structure
and dynamics of RNA and RNA–protein complexes. Mirko is particularly
interested in using novel isotope labeling methodology in conjunction
with tailored NMR experiments to provide new avenues to determine the
structure of very large RNA molecules.
James R. Williamson, who studies the structure and dynamics of
RNA molecules and RNA-protein complexes involved in the regulation of
gene expression by employing NMR spectroscopy and X-ray crystallography
for solving high-resolution three-dimensional structures and examining
the mechanism of assembly of multiprotein-RNA complexes.
Peter Wright, who uses high-resolution, multi-dimensional, hetero-nuclear
NMR spectroscopy to study protein and enzyme dynamics, protein folding,
and molecular recognition. In particular, his laboratory solves structures
of many protein-DNA and protein-protein complexes involved in the regulation
of transcription.
Kurt Wüthrich, who develops NMR methodologies, pioneering
the new techniques of transverse relaxation-optimized spectroscopy NMR
(TROSY) and cross-correlated relaxation-enhanced polarization transfer
(CRINEPT), which extend several-fold the size limit of structures that
can be solved with NMR. In addition, he solves many structures of biological
molecules—including pheromone, prion, and membrane proteins.
"Kurt's prize is extremely important because it is recognition for NMR
as a method for determining the structures of biological macromolecules
in solution," says Wright. "It really puts the field on the map, and having
him join the group of NMR structural biologists at TSRI brings additional
strength to what was already a world-class operation."
Wüthrich is Cecil H. and Ida M. Green Visiting Professor of Structural
Biology in the Department of Molecular Biology at The Scripps Research
Institute (TSRI); a member of TSRI's Skaggs Institute for Chemical Biology;
and Professor of Biophysics at Eidgenössische Technische Hochschule
Zürich (ETHZ) in Switzerland.
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