TY  - JOUR
AU  - Calandrini, V.
AU  - Dreyer, J.
AU  - Ippoliti, E.
AU  - Carloni, P.
TI  - Hydration of chloride anions in the NanC Porin from Escherichia coli: A comparative study by QM/MM and MD simulations
JO  - The journal of chemical physics
VL  - 141
IS  - 22
SN  - 1089-7690
CY  - Melville, NY
PB  - American Institute of Physics
M1  - FZJ-2015-03619
SP  - 22D521 -
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000346272800068
C6  - pmid:25494792
DO  - DOI:10.1063/1.4901111
UR  - https://juser.fz-juelich.de/record/201314
ER  -