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  Home > JCE Print > Journal of Chemical Education > Issues > 2003  > February  >
Chemical Education Today
Report: Nobel Prize in Chemistry, 2002
Using NMR to Determine Protein Structure in Solution
Silvia Cavagnero
Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706
Cover
February 2003
Vol. 80 No. 2
p. 125
Abstract
Nuclear magnetic resonance (NMR) is a marvelous spectroscopic technique that chemists, physicists, and biochemists routinely employ for their research around the world. This year half of the Nobel Prize for chemistry went to Kurt Wüthrich, who was recognized for the development of NMR-based techniques that lead to the structure determination of biomolecules in solution. In addition to implementing novel pulse sequences and software packages, Wüthrich also applied his methods to several biological systems of key importance to human health. These include the prion protein, which is heavily involved in the spongiform encephalopathy (best known as 'mad cow disease'), which recently caused numerous human deaths, particularly in the UK, due to ingestion of contaminated meat. Transverse relaxation optimized spectroscopy (TROSY) is the most intriguing new NMR method recently developed by Wüthrich and coworkers. This and other closely related pulse sequences promise to play a pivotal role in the extension of NMR to the conformational analysis of very large (up to the megadalton range) macromolecules and macromolecular complexes. More exciting new developments are expected in the near future.
More Information
*  Citation
 Cavagnero, Silvia. J. Chem. Educ. 2003 80 125.
*  Keywords
 Molecular Properties / Structure; NMR Spectrometry; Nuclear Overhauser Effect*; Proteins / Peptides; TROSY*
*  History
 Created:
Last Updated:		 January 6, 2003
February 28, 2005
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