In:
FEBS Letters, Wiley, Vol. 213, No. 2 ( 1987-03-23), p. 283-288
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(87)81506-5
Language:
English
Publisher:
Wiley
Publication Date:
1987
detail.hit.zdb_id:
1460391-3
SSG:
12
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