Structural involvement of carboxyl residues in the photocycle of bacteriorhodopsin
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(81)80910-6/fullpdf
Reference31 articles.
1. Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site
2. Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium
3. Three-dimensional model of purple membrane obtained by electron microscopy
4. Experimental evidence for secondary protein-chromophore interactions at the Schiff base linkage in bacteriorhodopsin: Molecular mechanism for proton pumping
5. Tunable Laser Resonance Raman Spectroscopy of Bacteriorhodopsin
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1. Substrate protection against inactivation of the mammalian polyamine-transport system by 1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide;Biochemical Journal;1996-10-01
2. The action of carboxyl modifying reagents on the ryanodine receptor/Ca2+release channel of skeletal muscle sarcoplasmic reticulum;Molecular Membrane Biology;1996-01
3. Role of carboxyl residues and membrane lipids in cation binding to bacteriorhodopsin;Archives of Biochemistry and Biophysics;1989-03
4. The bacteriorhodopsin proton pump: Effect of crosslinkings of lysine residues;Archives of Biochemistry and Biophysics;1988-02
5. Inhibition of the catalytic subunit of cAMP-dependent protein kinase by dicyclohexylcarbodiimide;Biochemistry;1987-11-01
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