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- W2337789849 abstract "Outer membrane protein G (OmpG), a monomeric beta-barrel membrane protein, has the potential to be used as a nano-sensor device. To achieve this goal, it is important to understand OmpG's ion current conducting properties. Previous studies have demonstrated pH-dependent gating, namely, current flow through the porin decreases as the pH decreases. While it is thought that loop regions have strong influence on the OmpG gating state, there is uncertainty on the mechanism that induces the functional switch as the pH is altered. Based on the DiSGro method of protein loop modeling, we extensively sample the three-dimensional conformations of multiple interacting loop regions of OmpG at various pH levels. Specifically, 10,000 loop samples are generated at pH 5 and pH 7 for each of 6 mutant OmpG variants and the wild type. These loops are used to study the conformations of mutant OmpG variants with experimentally observed differences in gating properties." @default.
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- W2337789849 date "2016-02-01" @default.
- W2337789849 modified "2023-09-26" @default.
- W2337789849 title "Computational Models of Interacting Loop Regions in pH-Dependent Gating of OmpG" @default.
- W2337789849 doi "https://doi.org/10.1016/j.bpj.2015.11.380" @default.
- W2337789849 hasPublicationYear "2016" @default.
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