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@ARTICLE{Calandrini:201314,
author = {Calandrini, V. and Dreyer, J. and Ippoliti, E. and Carloni,
P.},
title = {{H}ydration of chloride anions in the {N}an{C} {P}orin from
{E}scherichia coli: {A} comparative study by {QM}/{MM} and
{MD} simulations},
journal = {The journal of chemical physics},
volume = {141},
number = {22},
issn = {1089-7690},
address = {Melville, NY},
publisher = {American Institute of Physics},
reportid = {FZJ-2015-03619},
pages = {22D521 -},
year = {2014},
abstract = {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.},
cin = {GRS / IAS-5 / INM-9},
ddc = {540},
cid = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330 /
I:(DE-Juel1)INM-9-20140121},
pnm = {899 - ohne Topic (POF2-899)},
pid = {G:(DE-HGF)POF2-899},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000346272800068},
pubmed = {pmid:25494792},
doi = {10.1063/1.4901111},
url = {https://juser.fz-juelich.de/record/201314},
}