Open AccessTritium thermal activation study of bacteriorhodopsin topography
Author(s) -
TSETLIN Victor I.,
ALYONYCHEVA Tatya.,
SHEMYAKIN Vladimir V.,
NEIMAN Lev A.,
IVANOV Vadim T.
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14437.x
Subject(s) - bacteriorhodopsin , tritium , chemistry , membrane , transmembrane protein , amino acid , edman degradation , transmembrane domain , peptide , halobacterium , amino acid residue , biophysics , peptide sequence , biochemistry , biology , physics , nuclear physics , receptor , gene
The action of thermally activated tritium on the purple membrane and delipidated bacteriorhodopsin fragments has been studied, tritium incorporation into specified amino acid residues being quantified by Edman degradation. The membrane environment was found to affect the accessibility of amino acid residues for tritium. Bacteriorhodopsin fragments 14–31, 45–63, 81–89, 171–179, and 210–225 were localized to the membrane interior while fragments 4–12, 32–44, 64–65, 73–80, and 156–170 should lie outside or close to membrane surface. It was demonstrated that the peptide fragments joining transmembrane rods are not fully exposed to the solution.