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- W2004203897 abstract "The outer membrane of Gram-negative bacteria is a highly specialized structure that lies outside the cytoplasmic membrane and peptidoglycan layer and forms the interface between the cell and its external environment. The outer membrane constitutes a physical and functional barrier between the cell body and its surroundings which effectively controls access of solutes and external agents to the cytoplasmic membrane. The main function of OmpF is to facilitate the translocation of hydrophilic solutes with molecular mass upto 600 Da across the outer membrane. Ion selectivity, the property of porins in distinguishing charged ions is greatly affected by the electrostatics due to the presence of acidic and basic amino acid residues in the pore constriction zone. Detailed experimental and theoretical approaches including MD, BD and continuum electrodiffusion modeling revealed the importance of electrostatic interactions on the transport of cations and anions across the channel. Several computational studies have identified separate pathways for the flow of cations and anions along the OmpF pore. To probe this prediction experimentally, we report here the results from anomalous X-ray scattering data from rubidium and bromide revealing the permeation of cations and anions along the entire length of the OmpF channel." @default.
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- W2004203897 date "2013-01-01" @default.
- W2004203897 modified "2023-10-16" @default.
- W2004203897 title "Permeation Pathways of Cations and Anions in the OmpF Porin Channel using Anomalous X-Ray Scattering" @default.
- W2004203897 doi "https://doi.org/10.1016/j.bpj.2012.11.1030" @default.
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