Kurt Wuthrich is the Swiss scientist who, with John B. Fenn and Tanaka Koichi, won the Nobel Prize for Chemistry in 2002 for developing techniques to identify and analyze proteins and other large biological molecules.
After receiving a Ph.D. in organic chemistry from the University of Basel in 1964, Kurt Wuthrich took his postdoctoral training in Switzerland and the United States. In 1969 Kurt Wuthrich joined the Swiss Federal Institute of Technology, where he became a professor of biophysics in 1980. In 2001 he joined Scripps Research Institute in La Jolla, California, as a visiting professor.
In the early 1980s Kurt Wuthrich began devising a way to apply nuclear magnetic resonance (NMR) to the study of large biological molecules. Developed in the late 1940s, NMR provides detailed information about a molecule’s structure (whereas mass spectrometry is better suited for revealing kinds and amounts of molecules). NMR requires placing a sample in a very strong magnetic field and bombarding it with radio waves. The nuclei of certain atoms, such as hydrogen, in the molecules respond by emitting their own radio waves, which can be analyzed to work out their structural details.
At the time when Kurt Wuthrich began his research, NMR worked best on small molecules. Following the deciphering of the genetic code and the exploration of gene sequences, the study of proteins, which are large molecules, took on great importance. When using NMR on large molecules, however, the numerous atomic nuclei present produced an indecipherable tangle of radio signals. Wuthrich‘s solution, called sequential assignment, sorts out the tangle by methodically matching up each NMR signal with the corresponding hydrogen nucleus in the protein being analyzed. He also showed how to use that information to determine distances between numerous pairs of hydrogen nuclei and thereby build up a three-dimensional picture of the molecule. The first complete determination of a protein structure with Wuthrich‘s method was achieved in 1985, and about 20 percent of protein structures known by 2002 had been determined with NMR.