pH-Dependent absorption spectrum of a protein: a minimal electrostatic model of Anabaena sensory rhodopsin - Archive ouverte HAL Access content directly
Journal Articles Physical Chemistry Chemical Physics Year : 2017

pH-Dependent absorption spectrum of a protein: a minimal electrostatic model of Anabaena sensory rhodopsin

Elisa Pieri
  • Function : Author
Vincent Ledentu
  • Function : Author
Nicolas Ferre

Abstract

A minimal electrostatic model is introduced which aims at reproducing and analyzing the visible- light absorption energy shift of a protein with pH. It relies on the existence of a protein structure, the prediction of titratable amino-acid pKa values and a very limited set of parameters. Applied to the case of the photochromic Anabaena sensory rhodopsin protein, the model succeeds in reproducing qualitatively the reported experimental data, confirming the importance of aspartic acid 217 in the observed blue shift in the lambda(max) of ASR at neutral pH. It also suggests for the first time the role of two other amino acids, glutamic acid 36 at basic pH and aspartic acid 120 at acidic pH.
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hal-01774207 , version 1 (23-04-2018)

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Michael Stenrup, Elisa Pieri, Vincent Ledentu, Nicolas Ferre. pH-Dependent absorption spectrum of a protein: a minimal electrostatic model of Anabaena sensory rhodopsin. Physical Chemistry Chemical Physics, 2017, 19 (21), pp.14073--14084. ⟨10.1039/c7cp00991g⟩. ⟨hal-01774207⟩
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