Kurt Wüthrich

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Kurt Wüthrich lecturing at the 2005 European Forum held in Alpbach, Austria.

Kurt Wüthrich (born October 4, 1938) is a Swiss chemist and Nobel laureate.

Born in Aarberg, Switzerland, Wüthrich was educated in chemistry, physics, and mathematics at the University of Berne before pursuing his Ph.D. under the direction of Silvio Fallab at the University of Basel, awarded in 1964. He continued post-doctoral work with Fallab for a short time before leaving to work at the University of California, Berkeley from 1965 to 1967 with Robert E. Connick. That was followed by a stint working with Robert G. Shulman at the Bell Telephone Laboratories in Murray Hill, New Jersey (1967-1969).

Wüthrich returned to Switzerland, to Zurich, in 1969, where he began his career there at the ETH Zurich, rising to Professor of Biophysics by 1980. He currently maintains a laboratory there, although his appointment is at The Scripps Research Institute, in La Jolla, California.

[edit] Scientific work

During his graduate studies Wüthrich started out working with electron paramagnetic resonance spectroscopy an the subject of his Ph.D. thesis was "the catalytic activity of copper compounds in autoxidation reactions". During his time as a postdoc in Berkeley he began working with the newly developed and related technique of nuclear magnetic resonance spectroscopy to study the hydration of metal complexes. When Wüthrich joined the Bell Labs, he was put in charge of one of the first superconducting NMR spectrometers, and started studying the structure and dynamics of proteins. He has pursued this line of research ever since.

After returning to Switzerland, Wüthrich collabrated with among others nobel laureate Richard R. Ernst on developing the first 2 dimensional NMR experiments, and established the nuclear Overhauser effect as a convinient way of measuring distances within proteins. This research later led to the complete assignment and of resonances for among others the bovine pancreatic trypsin inhibitor and glucagon.

He was awarded part of the Nobel Prize in Chemistry in 2002 for his leadership of ongoing work, begun in the 1970s, on the use of multidimensional nuclear magnetic resonance spectroscopy to study the structure of proteins.