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Bovine rhodopsin was isolated in the unbleached form as a retinal disc membrane suspension and spin-labelled with 4-maleimido-2,2,6,6-tetramethylpiperidine-N-oxyl. Both conventional and saturation transfer electron spin resonance methods were used to investigate the sensitivity of the spin-label to conformational changes of rhodopsin induced by both transient and long-term exposure to light. The results indicate that the ESR methods do display sensitivity to such changes. An exponential decay curve with a time constant of 10 s was obtained by following the height of a single peak in the saturation transfer electron spin resonance spectrum in response to a single light flash.


Journal article


Biochem Biophys Res Commun

Publication Date





1412 - 1417


Animals, Cattle, Cyclic N-Oxides, Electron Spin Resonance Spectroscopy, Light, Protein Conformation, Retinal Pigments, Rhodopsin, Spin Labels