Testing the Force Response of the Allosteric Cycle of Myosin VI using Brownian Dynamics

Abstract

A central question in the study of many processive motor proteins is how are the mechano-chemical cycles in the two motor domains coordinated. In our study, we investigate the hypothesis that the coordination is achieved via subtle changes in the reaction rates due to asymmetric tension within the structures. We perform coarse-grained Brownian dynamics simulations of the myosin VI motor domain and study structural changes in the nucleotide binding pocket as a function of applied tension and relate the structural changes to the changes in the chemical reaction rates.