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Kurt Wüthrich, the ETH Zürich, and the Development of NMR Spectroscopy for the Investigation of Structure, Dynamics, and Folding of Proteins
Author(s) -
Schwalbe Harald
Publication year - 2003
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200390023
Subject(s) - nuclear magnetic resonance spectroscopy , folding (dsp implementation) , macromolecule , chemistry , spectroscopy , polymer science , physics , stereochemistry , engineering , biochemistry , electrical engineering , quantum mechanics
Spinning to the top : In 2002, the Nobel prize committee awarded one half of the Nobel prize in Chemistry to Prof. Kurt Wüthrich, of the Eidgenössische Technische Hochschule Zürich, “for his development of nuclear magnetic resonance spectroscopy for determining the three‐dimensional structure of biological macromolecules in solution.” This Minireview summarizes Wüthrich's scientific contributions to this field and tells the story of the development of NMR spectroscopy for the study of biological macromolecules in general and of proteins (see picture) in particular.