Premium
19 F NMR study of 5‐fluorotryptophan‐labeled bacteriorhodopsin
Author(s) -
Arseniev A.S.,
Kuryatov A.B.,
Tsetlin V.I.,
Bystrov V.F.,
Ivanov V.T.,
Ovchinnikov Yu.A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81506-5
Subject(s) - bacteriorhodopsin , chemistry , proteolysis , tryptophan , nuclear magnetic resonance spectroscopy , stereochemistry , carbon 13 nmr , crystallography , cleavage (geology) , proton nmr , membrane , biochemistry , enzyme , amino acid , biology , paleontology , fracture (geology)
19 F NMR and CD spectra reveal that bacteriorhodopsin as well as its 5‐fluorotryptophan‐labeled analog solubilized in a CH 3 OH‐CHCl 3 mixture (i) retains a secondary structure of the fully active chromoprotein in the purple membrane and (ii) possesses a folded structure in which modifications at the Lys‐216 bound retinal are sensed by sequentially remote tryptophan residues. Individual fragments isolated after limited proteolysis and NaBH 4 ‐cleavage of bacteriorhodopsin keep the spatial structure of the intact polypeptide chain in the organic solvent.