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Membrane proteins as light‐energy transducers
Author(s) -
Ovchinnikov Yu. A.
Publication year - 1985
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360240113
Subject(s) - bacteriorhodopsin , transducin , chemistry , rhodopsin , protein subunit , membrane , amino acid residue , protein secondary structure , amino acid , peptide sequence , membrane protein , proteolysis , biophysics , biochemistry , enzyme , biology , retinal , gene
Abstract Monoclonal antibodies to different parts of bacteriorhodopsin were raised to define its topography in the membrane. It is shown that the amino acid residue Glu 194 is a part of an antigenic determinant and should be located on the membrane surface. We found that the removal of the C‐terminal 17 amino acid sequence does not affect the efficiency of the proton transport in bacteriorhodopsin. From a combination of proteolysis and secondary structure prediction methods an experimentally testable structural model for bovine rhodopsin is presented. The complete amino acid sequence of the transducin γ‐subunit consisting of 69 residues was determined.