19 F NMR study of 5‐fluorotryptophan‐labeled bacteriorhodopsin
1987; Wiley; Volume: 213; Issue: 2 Linguagem: Inglês
10.1016/0014-5793(87)81506-5
ISSN1873-3468
AutoresAlexander S. Arseniev, Alexander Kuryatov, Victor I. Tsetlin, V. F. Bystrov, В. Т. Иванов, Yu.A. Ovchinnikov,
Tópico(s)Mass Spectrometry Techniques and Applications
Resumo19 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.
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