Dynamical control by water at a molecular level in protein dimer association and dissociation.

ABSTRACT: Water, often termed as the "lubricant of life," is expected to play an active role in navigating protein dissociation-association reactions. In order to unearth the molecular details, we first compute the free-energy surface (FES) of insulin dimer dissociation employing metadynamics simulation, and then carry out analyses of insulin dimerization and dissociation using atomistic molecular-dynamics simulation in explicit water. We select two sets of initial configurations from 1) the dissociated state and 2) the transition state, and follow time evolution using several long trajectories (∼1-2 μs). During the process we not only monitor configuration of protein monomers, but also the properties of water. Although the equilibrium structural properties of water between the two monomers approach

SUBMITTER: Banerjee P 

PROVIDER: S-EPMC7007538 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature