Electronic Polarizability Tunes the Function of the Human Bestrophin 1 Cl^- Channel.

ABSTRACT: Mechanisms of anion permeation within ion channels and nanopores remain poorly understood. Recent cryo-electron microscopy structures of the human bestrophin 1 Cl^- channel (hBest1) provide an opportunity to evaluate ion interactions predicted by molecular dynamics (MD) simulations against experimental observations. Here, we implement the fully polarizable force field AMOEBA in MD simulations on different conformations of hBest1. This force field models multipole moments up to the quadrupole. Using this approach, we model key biophysical properties of the channel that can only be simulated when electronic polarization is included in the molecular models and show that Cl^- permeation through the neck of the pore is achieved through hydrophobic solvation concomitant with

SUBMITTER: Phan LX 

PROVIDER: S-EPMC11780730 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature