Saturation transfer electron paramagnetic resonance on membrane-bound proteins. I-rotational diffusion of rhodopsin in the visual receptor membrane

Anne Baroin, David D. Thomas, Beverley Osborne, Philippe F. Devaux

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

We have applied the technique of saturation transfer electron paramagnetic resonance to the study of spin labeled membrane-bound bovine rhodopsin. Based on the comparison with theoretical and experimental spectra corresponding to isotropic slow motion, the present data leads to a rotational correlation time for the membrane-bound rhodopsin molecule of 20 μsec at 20°C. Bleaching does not appear to influence the motion of the protein while addition of glutaraldehyde (5%) stops its rotation completely. These results are in good agreement with what is known about the motion of the membrane-bound rhodopsin, establishing the applicability of the saturation transfer technique to the study of slow anisotropic motions of membrane-bound proteins.

Original languageEnglish (US)
Pages (from-to)442-447
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume78
Issue number1
DOIs
StatePublished - Sep 9 1977
Externally publishedYes

Bibliographical note

Funding Information:
This work was SuoDorted bv grants from the DGRST( commission Memknes Biblggiques).

Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.

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