Water dynamics in protein hydration shells: the molecular origins of the dynamical perturbation.

ABSTRACT: Protein hydration shell dynamics play an important role in biochemical processes including protein folding, enzyme function, and molecular recognition. We present here a comparison of the reorientation dynamics of individual water molecules within the hydration shell of a series of globular proteins: acetylcholinesterase, subtilisin Carlsberg, lysozyme, and ubiquitin. Molecular dynamics simulations and analytical models are used to access site-resolved information on hydration shell dynamics and to elucidate the molecular origins of the dynamical perturbation of hydration shell water relative to bulk water. We show that all four proteins have very similar hydration shell dynamics, despite their wide range of sizes and functions, and differing secondary structures. We demonstrate that this

SUBMITTER: Fogarty AC 

PROVIDER: S-EPMC4103960 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature