Origin of pK_a Shifts of Internal Lysine Residues in SNase Studied Via Equal-Molar VMMS Simulations in Explicit Water.

ABSTRACT: Protein internal ionizable groups can exhibit large shifts in pK_a values. Although the environment and interaction changes have been extensively studied both experimentally and computationally, direct calculation of pK_a values of these internal ionizable groups in explicit water is challenging due to energy barriers in solvent interaction and in conformational transition. The virtual mixture of multiple states (VMMS) method is a new approach designed to study chemical state equilibrium. This method constructs a virtual mixture of multiple chemical states in order to sample the conformational space of all states simultaneously and to avoid crossing energy barriers related to state transition. By applying VMMS to 25 variants of staphylococcal nuclease with lysine residu

SUBMITTER: Wu X 

PROVIDER: S-EPMC6415756 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature