Charge transport modification exhibiting an increase of conductance activated by an external green light in Bacteriorhodopsin is correlated to its conformational change. A theoretical model based on a map of the protein  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 and provides for the potential barriers involved in the charge transfer an average height of 69 meV over an interacting radius of 6 \aa . The predictability of the model is also tested on bovine rhodopsin, the prototype of the G protein coupled receptor (GPCR) family also sensitive to the light, with results exhibiting the opposite behaviour of a decrease of conductance in the presence of light.
When moving from native to light activated bacteriorhodopsin, 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.
R
Charge transport modification exhibiting
When moving from native to light activated bacteriorhodopsin, modification of charge transport consisting of
D
activated by an external green light in Bacteriorhodopsin
R
its
the protein
A
tertiary
R
amino-acids
amino acids
D
and provides for the potential barriers involved in the charge transfer an average height of 69 meV over an interacting radius of 6 \aa
R
also
further
R
the prototype of the G protein
a G-protein
D
family
R
the light, with results exhibiting the opposite behaviour of
light. In this case, results show an opposite behaviour with