PEPTIDE MODELS FOR THE BACTERIORHODOPSIN CHROMOPHORE. RETINYLIDENE‐LYSINE SYSTEMS CONTAINING ASPARTIC ACID AND SERINE RESIDUES
- 1 May 1984
- journal article
- research article
- Published by Wiley in Photochemistry and Photobiology
- Vol. 39 (5) , 667-672
- https://doi.org/10.1111/j.1751-1097.1984.tb03907.x
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- Symmetric charge distribution in the bacteriorhodopsin binding siteJournal of the American Chemical Society, 1983
- A remarkable blue shift of retinal protonated Schiff base due to electrostatic interaction of positive chargesJournal of the Chemical Society, Chemical Communications, 1983
- Structural Basis of Proton-Translocating Protein FunctionAnnual Review of Biophysics and Bioengineering, 1982
- The identification of Lys216 as the retinal binding residue in bacteriorhodopsinFEBS Letters, 1981
- Lysine 216 is a binding site of the retinyl moiety in bacteriorhodopsinFEBS Letters, 1981
- SPECTROSCOPY OF POLYENES–III. ABSORPTION AND EMISSION SPECTRAL INVESTIGATION OF POLYENE SCHIFF BASES AND PROTONATED SCHIFF BASES RELATED TO VISUAL PIGMENTSPhotochemistry and Photobiology, 1979
- The structural basis of the functioning of bacteriorhodopsin: An overviewFEBS Letters, 1979
- Resonance Raman studies of the purple membraneBiochemistry, 1977
- SOLVENT EFFECTS ON THE SPECTRA OF RETINAL SCHIFF BASES—11. MODELS FOR CONVERGENCE AND CLUSTERING OF VISUAL PIGMENT SPECTRA*Photochemistry and Photobiology, 1977
- SOLVENT EFFECTS ON THE SPECTRA OF RETINAL SCHIFF BASES—I. MODELS FOR THE BATHOCHROMIC SHIFT OF THE CHROMOPHORE SPECTRUM IN VISUAL PIGMENTS*Photochemistry and Photobiology, 1977