[Possible determination of the structural organization of bacterial and animal rhodopsins by the hydrophobicity of amino acid residues].

Abstract

From a comparative analysis of the distribution of hydrophobicity in bacterial and animal (bovine) rhodopsins, the following peculiarities in the structure of these proteins have been assumed: 1) each of these proteins has 5 hydrophobic regions of equal length (20-28 residues) able to be arranged across the membrane and one region of doubled length. 2) The… (More)

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Cite this paper

@article{Tarakhovski1984PossibleDO, title={[Possible determination of the structural organization of bacterial and animal rhodopsins by the hydrophobicity of amino acid residues].}, author={Iu S Tarakhovskiĭ}, journal={Biofizika}, year={1984}, volume={29 3}, pages={383-8} }