Fourier Transform Infrared Difference Spectra of Intermediates in Rhodopsin Bleaching
- 18 March 1983
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 219 (4590) , 1333-1335
- https://doi.org/10.1126/science.6828860
Abstract
The membrane protein rhodopsin is the primary light receptor in vision. Fourier transform infrared difference spectroscopy is sensitive to conformational changes in both the protein and the retinylidene chromophore of rhodopsin. By blocking rhodopsin bleaching at specific intermediates, it is possible to elucidate some of the primary molecular events of vision.This publication has 22 references indexed in Scilit:
- Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopyPublished by Elsevier ,2005
- Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsinBiochemistry, 1982
- ASSIGNING THE RESONANCE RAMAN SPECTRAL FEATURES OF RHODOPSIN, ISORHODOPSIN AND BATHORHODOPSIN IN BOVINE PHOTOSTATIONARY STATE SPECTRA‡Photochemistry and Photobiology, 1979
- Visual Transduction in Vertebrate PhotoreceptorsAnnual Review of Neuroscience, 1979
- Resonance Raman studies of bovine metarhodopsin I and metarhodopsin IIBiochemistry, 1978
- Spectral studies on the conformation of rhodopsinEuropean Biophysics Journal, 1977
- Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsinJournal of Molecular Biology, 1977
- Resonance Raman spectroscopy of rhodopsin in retinal disk membranesBiochemistry, 1974
- The Molecular Basis of Visual ExcitationNature, 1968
- Pre-Lumirhodopsin and the Bleaching of Visual PigmentsNature, 1963