Probing Transient Conformational States of Proteins by Solid‐State R1ρ Relaxation‐Dispersion NMR Spectroscopy |
| |
| Authors: | Dr. Peixiang Ma Jens D. Haller Jérémy Zajakala Dr. Pavel Macek Dr. Astrid C. Sivertsen Prof. Dr. Dieter Willbold Dr. Jérôme Boisbouvier Dr. Paul Schanda |
| |
| Affiliation: | 1. Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), CEA, DSV, IBS, 38027 Grenoble (France);2. CNRS, IBS, 38027 Grenoble (France);3. Institut für Physikalische Biologie, Heinrich‐Heine‐Universt?t Düsseldorf (Germany);4. ICS‐6: Structural Biochemistry, Forschungszentrum Jülich (Germany) |
| |
| Abstract: | 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. |
| |
| Keywords: | protein dynamics relaxation dispersion solid‐state NMR spectroscopy transient conformations ubiquitin |
|
|
