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- W2066832022 abstract "Significance Voltage sensors are integral membrane protein domains that regulate ion channels and enzymes by transporting electrically charged residues across a narrow constriction that focuses the membrane electrical field. Here, we investigated how this constriction, also called the “gating pore,” controls this transport by studying the effects of a large number of point mutations. Our analysis indicates the presence of nonambiguous statistical correlations between specific amino acid lateral-chain physicochemical properties (size, hydrophobicity) and specific functional features of the voltage sensor (voltage sensitivity and transport kinetics). This study allowed us to propose engineering-like mechanisms by which gating pore residues control the voltage sensor operation." @default.
- W2066832022 created "2016-06-24" @default.
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- W2066832022 date "2014-04-29" @default.
- W2066832022 modified "2023-10-13" @default.
- W2066832022 title "Moving gating charges through the gating pore in a Kv channel voltage sensor" @default.
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- W2066832022 doi "https://doi.org/10.1073/pnas.1406161111" @default.
- W2066832022 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4024920" @default.
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