E Alfinito, J Pousset, L Reggiani, K Lee
The increasing interest in photoactivated proteins as natural replacement of standard inorganic materials in photocells drives to the compared analysis of bacteriorhodopsin and proteorhodopsin, two widely diffused proteins belonging to the family of \textit{type-1} opsins. These proteins share similar behaviours but exhibit relevant differences in the sequential chain of the amino acids constituting their tertiary structure. The use of an impedance network analogue to model the protein main features provides a microscopic interpretation of a set of experiments on their photoconductance properties. In particular, this model links the protein electrical responses to the tertiary structure and to the interactions among neighbouring amino acids. The same model is also used to predict the small-signal response in terms of the Nyquist plot. Interesting enough, these rhodopsins are found to behave like a wide gap semiconductor with intrinsic conductivities of the order of $10^{-7}$ S/cm.
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http://arxiv.org/abs/1306.5963
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