Opsin Structure Probed by Raman Spectroscopy of Photoreceptor Membranes
- 19 March 1976
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 191 (4232), 1176-1178
- https://doi.org/10.1126/science.1257742
Abstract
The first nonresonance Raman spectra of photoreceptor membranes are presented. Information about the membrane protein, opsin, and the membrane phospholipids can be deduced. Opsin appears to contain alpha-helical structure but little beta structure. The tyrosine residues are predominantly hydrogen bonded, and disulfide bonds, if they are present, are not in the normal gauche-gauche configuration.This publication has 32 references indexed in Scilit:
- Bacteriorhodopsin: A trans-membrane pump containing α-helixJournal of Molecular Biology, 1975
- The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction patternJournal of Molecular Biology, 1975
- Conformation of the cystine linkages in bovine α-lactalbumin as revealed by its Raman effectJournal of Molecular Biology, 1974
- Raman spectroscopic study of the valinomycin-KSCN complexJournal of Molecular Biology, 1974
- Laser-excited Raman spectroscopy of biomolecules. VI. Polypeptides as conformational modelsJournal of the American Chemical Society, 1974
- Ion Fluxes in Disk Membranes of Retinal Rod Outer SegmentsNature, 1974
- Lateral diffusion of rhodopsin in Necturus rodsExperimental Eye Research, 1973
- Vertebrate rod outer segment membranesBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1973
- Tunable laser resonance Raman spectroscopy of the visual process. I: The spectrum of rhodopsinJournal of Raman Spectroscopy, 1973
- Laser-excited Raman spectroscopy of biomolecules: II. Native ribonuclease and α-chymotrypsinJournal of Molecular Biology, 1970