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When moving from native to light activated bacteriorhodopsin, modification ofcharge transport consisting of an increase of conductance is correlated to theprotein conformational change. A theoretical model based on a map of theprotein tertiary structure into a resistor network is implemented to accountfor a sequential tunneling mechanism of charge transfer through neighbouringamino acids. The model is validated by comparison with current-voltageexperiments. The predictability of the model is further tested on bovinerhodopsin, a G-protein coupled receptor (GPCR) also sensitive to light. In thiscase, results show an opposite behaviour with a decrease of conductance in thepresence of light.

Charge transport in bacteriorhodopsin monolayers: The contribution of conformational change to current-voltage characteristics