How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?

ABSTRACT: The dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments-where the sample is transferred to low fields for longitudinal (T₁) relaxation, and back to high field for detection with residue-specific resolution-seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the "detector" analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-1

SUBMITTER: Smith AA 

PROVIDER: S-EPMC8018934 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature