Elucidation of the Nature of the Conformational Changes of the EF-interhelical Loop in Bacteriorhodopsin and of the Helix VIII on the Cytoplasmic Surface of Bovine Rhodopsin: A Time-resolved Fluorescence Depolarization Study-Reference-Cited by-同舟云学术

Elucidation of the Nature of the Conformational Changes of the EF-interhelical Loop in Bacteriorhodopsin and of the Helix VIII on the Cytoplasmic Surface of Bovine Rhodopsin: A Time-resolved Fluorescence Depolarization Study

Published:2003-05 Issue:3 Volume:328 Page:705-719
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Alexiev U.,Rimke I.,Pöhlmann T.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference45 articles.

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4. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin;Otto;Proc. Natl Acad. Sci. USA,1989

5. Optical study of the light-induced protonation changes associated with the metarhodopsin II intermediate in rod-outer-segment membranes;Bennett;Eur. J. Biochem.,1980

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