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Microsecond Timescale Protein Dynamics: a Combined Solid‐State NMR Approach
Author(s) -
Rovó Petra,
Linser Rasmus
Publication year - 2018
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201701238
Subject(s) - microsecond , chemistry , chemical physics , magic angle spinning , molecule , protein dynamics , relaxation (psychology) , dispersion (optics) , molecular dynamics , chemical shift , excited state , solid state nuclear magnetic resonance , biological system , nuclear magnetic resonance spectroscopy , computational chemistry , crystallography , nuclear magnetic resonance , physics , stereochemistry , atomic physics , psychology , social psychology , organic chemistry , astronomy , optics , biology
Conformational exchange in proteins is a major determinant in protein functionality. In particular, the μs–ms timescale is associated with enzymatic activity and interactions between biological molecules. We show here that a comprehensive data set of R 1 ρ relaxation dispersion profiles employing multiple effective fields and tilt angles can be easily obtained in perdeuterated, partly back‐exchanged proteins at fast magic‐angle spinning and further complemented with chemical‐exchange saturation transfer NMR experiments. The approach exploits complementary sources of information and enables the extraction of multiple exchange parameters for μs–ms timescale conformational exchange, most notably including the sign of the chemical shift differences between the ground and excited states.