LOW TEMPERATURE RESONANCE RAMAN STUDY OF THE L INTERMEDIATE OF BACTERIORHODOPSIN
- 1 April 1981
- journal article
- Published by Wiley in Photochemistry and Photobiology
- Vol. 33 (4) , 567-571
- https://doi.org/10.1111/j.1751-1097.1981.tb05460.x
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Photoisomerization, energy storage, and charge separation: A model for light energy transduction in visual pigments and bacteriorhodopsinProceedings of the National Academy of Sciences, 1979
- Resonance Raman study of the dark-adapted form of the purple membrane proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Resonance Raman spectroscopy of the retinylidene chromophore in bacteriorhodopsin (bR570), bR560, M412, and other intermediates: structural conclusions based on kinetics, analogs, models, and isotopically labeled membranesBiochemistry, 1978
- Ultraviolet and visible absorption spectra of the purple membrane protein and the photocycle intermediatesBiochemistry, 1978
- More evidence that light isomerises the chromophore of purple membrane proteinNature, 1978
- Resonance Raman studies of the purple membraneBiochemistry, 1977
- Kinetic Resonance Raman Spectroscopy: Dynamics of Deprotonation of the Schiff Base of BacteriorhodopsinScience, 1977
- Improved Isolation Procedures for the Purple Membrane of Halobacterium HalobiumPreparative Biochemistry, 1975
- Tunable Laser Resonance Raman Spectroscopy of BacteriorhodopsinProceedings of the National Academy of Sciences, 1974
- Raman spectra of Schiff bases of retinal (models of visual photoreceptors)Journal of the American Chemical Society, 1971