Probing transient conformational states of proteins by solid-state R(1ρ) relaxation-dispersion NMR spectroscopy

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....

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2014-04, Vol.53 (17), p.4312-4317
Main Authors: Ma, Peixiang, Haller, Jens D, Zajakala, Jérémy, Macek, Pavel, Sivertsen, Astrid C, Willbold, Dieter, Boisbouvier, Jérôme, Schanda, Paul
Format: Article
Language:English
Subjects:
Deuterium - chemistry
Humans
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Proteins - chemistry
Protons
Thermodynamics
Ubiquitin - chemistry
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Summary: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 R1ρ 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.
ISSN:1521-3773
DOI:10.1002/anie.201311275