%0 Journal Article
%A Calandrini, V.
%A Dreyer, J.
%A Ippoliti, E.
%A Carloni, P.
%T Hydration of chloride anions in the NanC Porin from Escherichia coli: A comparative study by QM/MM and MD simulations
%J The journal of chemical physics
%V 141
%N 22
%@ 1089-7690
%C Melville, NY
%I American Institute of Physics
%M FZJ-2015-03619
%P 22D521 -
%D 2014
%X Chloride anions permeate the bacterial NanC porin in physiological processes. Here we present a DFT-based QM/MM study of this porin in the presence of these anions. Comparison is made with classical MD simulations on the same system. In both QM/MM and classical approaches, the anions are almost entirely solvated by water molecules. However, the average water–Cl− distance is significantly larger in the first approach. Polarization effects of protein groups close to Cl− anion are sizeable. These effects might modulate the anion-protein electrostatic interactions, which in turn play a central role for selectivity mechanisms of the channel.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000346272800068
%$ pmid:25494792
%R 10.1063/1.4901111
%U https://juser.fz-juelich.de/record/201314