Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.

ABSTRACT: Water dynamics on the protein surface mediate both protein structure and function. However, many questions remain about the role of the protein hydration layers in protein fluctuations and how the dynamics of these layers relate to specific protein properties. The fish eye lens protein γM7-crystallin (γM7) is found in vivo at extremely high concentrations nearing the packing limit, corresponding to only a few water layers between adjacent proteins. In this study, we conducted a site-specific probing of hydration water motions and side-chain dynamics at nine selected sites around the surface of γM7 using a tryptophan scan with femtosecond spectroscopy and NMR nuclear spin relaxation (NSR). We observed correlated fluctuations between hydration water and protein side chains on the time scales

SUBMITTER: Houston P 

PROVIDER: S-EPMC7261499 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature