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• W2063736872 abstract "Bacterial porins, which allow the passage of solutes across the outer bacterial membrane, are structurally well characterized. They therefore lend themselves to detailed studies of the determinants of ion flow through transmembraneous channels. In a comparative study, we have performed Brownian dynamics simulations to obtain statistically significant transfer efficiencies for cations and anions through matrix porin OmpF, osmoporin OmpK36, phosphoporin PhoE and two OmpF charge mutants. The simulations show that the electrostatic potential at the highly charged channel constriction serves to enhance ion permeability of either cations or anions, dependent on the type of porin. At the same time translocation of counterions is not severely impeded. At the constriction, cations and anions follow distinct trajectories, due to the segregation of basic and acidic protein residues. Simulated ion selectivity and relative conductance agree well with experimental values, and are dependent crucially on the charge constellation at the pore constriction. The experimentally observed decrease in ion selectivity and single channel conductance with increasing ionic strength is well reproduced and can be attributed to electrostatic shielding of the pore lining." @default.
• W2063736872 created "2016-06-24" @default.
• W2063736872 creator A5002943998 @default.
• W2063736872 creator A5062928050 @default.
• W2063736872 date "1999-12-01" @default.
• W2063736872 modified "2023-10-15" @default.
• W2063736872 title "Brownian dynamics simulation of ion flow through porin channels" @default.
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• W2063736872 doi "https://doi.org/10.1006/jmbi.1999.3326" @default.
• W2063736872 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10600374" @default.
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