Influence of electronic polarization on the binding of anions to a chloride-pumping rhodopsin.

ABSTRACT: The functional properties of some biological ion channels and membrane transport proteins are proposed to exploit anion-hydrophobic interactions. Here, we investigate a chloride-pumping rhodopsin as an example of a membrane protein known to contain a defined anion binding site composed predominantly of hydrophobic residues. Using molecular dynamics simulations, we explore Cl- binding to this hydrophobic site and compare the dynamics arising when electronic polarization is neglected (CHARMM36 [c36] fixed-charge force field), included implicitly (via the prosECCo force field), or included explicitly (through the polarizable force field, AMOEBA). Free energy landscapes of Cl- moving out of the binding site and into bulk solution demonstrate that the inclusion of polarization results in strong

SUBMITTER: Phan LX 

PROVIDER: S-EPMC10147828 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature