Publication Date:
2014-11-12
Description:
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.
Print ISSN:
0021-9606
Electronic ISSN:
1089-7690
Topics:
Chemistry and Pharmacology
,
Physics
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