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 language | English (US) |
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Pages (from-to) | 442-447 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 78 |
Issue number | 1 |
DOIs | |
State | Published - Sep 9 1977 |
Externally published | Yes |
Bibliographical note
Funding Information:This work was SuoDorted bv grants from the DGRST( commission Memknes Biblggiques).