The Structural and Dynamical Properties of the Hydration of SNase Based on a Molecular Dynamics Simulation.

ABSTRACT: The dynamics of protein-water fluctuations are of biological significance. Molecular dynamics simulations were performed in order to explore the hydration dynamics of staphylococcal nuclease (SNase) at different temperatures and mutation levels. A dynamical transition in hydration water (at ~210 K) can trigger larger-amplitude fluctuations of protein. The protein-water hydrogen bonds lost about 40% in the total change from 150 K to 210 K, while the Mean Square Displacement increased by little. The protein was activated when the hydration water in local had a comparable trend in making hydrogen bonds with protein- and other waters. The mutations changed the local chemical properties and the hydration exhibited a biphasic distribution, with two time scales. Hydrogen bonding relaxation govern

SUBMITTER: Liu H 

PROVIDER: S-EPMC8434405 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature