Probing Transient Conformational States of Proteins by Solid‐State R1ρ Relaxation‐Dispersion NMR Spectroscopy1. Issue 17 (18th March 2014)

• Record Type: Journal Article
• Authors: Ma, Peixiang; Haller, Jens D.; Zajakala, Jérémy; Macek, Pavel; Sivertsen, Astrid C.; Willbold, Dieter; Boisbouvier, Jérôme; Schanda, Paul
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 17(2014)
• Page Start: 4312
• Page End: 4317
• Publication Date: 2014-03-18
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201311275
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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.</p> </abstract>