Low-temperature solid-state carbon-13 NMR studies of the retinal chromophore in rhodopsin
- 28 February 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (6) , 1606-1611
- https://doi.org/10.1021/bi00380a018
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 11 references indexed in Scilit:
- Fourier-transform infrared difference spectroscopy of rhodopsin and its photoproducts at low temperatureBiochemistry, 1985
- NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motionBiochemistry, 1985
- Two-photon spectroscopy of locked-11-cis-rhodopsin: evidence for a protonated Schiff base in a neutral protein binding site.Proceedings of the National Academy of Sciences, 1985
- Solid-state carbon-13 NMR studies of retinal in bacteriorhodopsinBiochemistry, 1984
- Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases.Proceedings of the National Academy of Sciences, 1984
- Lipid bilayer dynamics and rhodopsin-lipid interactions: New approach using high-resolution solid-state 13C NMRBiochemical and Biophysical Research Communications, 1983
- Origins of inhomogeneous broadening in the vibronic spectra of visual chromophores and visual pigmentsJournal of the American Chemical Society, 1982
- A proton and carbon-13 nuclear magnetic resonance spectroscopy study of the conformation of a protonated 11-cis-retinal Schiff baseBiochemistry, 1979
- Shape and size of bovine rhodopsin: A small-angle X-ray scattering study of a rhodopsin-detergent complexJournal of Molecular Biology, 1976
- The structure of visual pigments. I. Carbon-13 nuclear magnetic resonance spectroscopy of N-all-trans-retinylidenepropylimine and its protonated speciesJournal of the American Chemical Society, 1976