The increasing interest in photoactivated proteins as natural replacements for standard inorganic materials in photocells leads to the comparison analysis of bacteriorhodopsin and proteorhodopsin, two widely diffused proteins belonging to the family of type-1 opsins. These proteins share similar behaviors but exhibit relevant differences in the sequential chain of the amino acids constituting their tertiary structure. The use of an impedance network analog to model the protein main features provides a microscopic interpretation of a set of experiments on their photo-conductance properties. In particular, this model links the protein electrical responses to the tertiary structure and to the interactions between neighboring amino acids. The same model is also used to predict the small-signal response in terms of the Nyquist plot. Interestingly, these rhodopsins are found to behave like a wide-gap semiconductor with intrinsic conductivities of the order of 107 S cm1.
Photoreceptors for a light biotransducer:...
ALFINITO, ELEONORA;POUSSET, JEREMY;REGGIANI, Lino;
2013-01-01
Abstract
The increasing interest in photoactivated proteins as natural replacements for standard inorganic materials in photocells leads to the comparison analysis of bacteriorhodopsin and proteorhodopsin, two widely diffused proteins belonging to the family of type-1 opsins. These proteins share similar behaviors but exhibit relevant differences in the sequential chain of the amino acids constituting their tertiary structure. The use of an impedance network analog to model the protein main features provides a microscopic interpretation of a set of experiments on their photo-conductance properties. In particular, this model links the protein electrical responses to the tertiary structure and to the interactions between neighboring amino acids. The same model is also used to predict the small-signal response in terms of the Nyquist plot. Interestingly, these rhodopsins are found to behave like a wide-gap semiconductor with intrinsic conductivities of the order of 107 S cm1.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
