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Probing Transient Conformational States of Proteins by Solid‐State R 1ρ Relaxation‐Dispersion NMR Spectroscopy
Author(s) -
Ma Peixiang,
Haller Jens D.,
Zajakala Jérémy,
Macek Pavel,
Sivertsen Astrid C.,
Willbold Dieter,
Boisbouvier Jérôme,
Schanda Paul
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201311275
Subject(s) - microsecond , relaxation (psychology) , spectroscopy , nuclear magnetic resonance spectroscopy , chemical physics , dispersion (optics) , chemistry , magic angle spinning , solid state nuclear magnetic resonance , crystallography , nuclear magnetic resonance , physics , stereochemistry , psychology , social psychology , astronomy , optics , quantum mechanics
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function. Many biomolecular reactions take place within microseconds to milliseconds, and this timescale is therefore of central functional importance. Here we show that R 1ρ relaxation dispersion experiments in magic‐angle‐spinning solid‐state NMR spectroscopy make it possible to investigate the thermodynamics and kinetics of such exchange process, and gain insight into structural features of short‐lived states.