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• W3102752687 endingPage "68002" @default.
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• W3102752687 abstract "When moving from native to light-activated bacteriorhodospin, modification of charge transport consisting of an increase of conductance is correlated to the protein conformational change. A theoretical model based on a map of the protein tertiary structure into a resistor network is implemented to account for a sequential tunneling mechanism of charge transfer through neighbouring amino acids. The model is validated by comparison with current-voltage experiments. The predictability of the model is further tested on bovine rhodopsin, a G-protein coupled receptor (GPCR) also sensitive to light. In this case, results show an opposite behaviour with a decrease of conductance in the presence of light." @default.
• W3102752687 created "2020-11-23" @default.
• W3102752687 creator A5061882387 @default.
• W3102752687 creator A5088216454 @default.
• W3102752687 date "2009-03-01" @default.
• W3102752687 modified "2023-09-26" @default.
• W3102752687 title "Charge transport in bacteriorhodopsin monolayers: The contribution of conformational change to current-voltage characteristics" @default.
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• W3102752687 doi "https://doi.org/10.1209/0295-5075/85/68002" @default.
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