Regeneration of Rhodopsin and Bacteriorhodopsin
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چکیده
منابع مشابه
Photoaffinity labeling of rhodopsin and bacteriorhodopsin.
Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophor...
متن کاملStudies in rhodopsin. VI. Regeneration of rhodopsin.
reducing power of steroids. The low pH of the reagent, which is responsible for hydrolysis of the cellulose, cannot be raised materially without seriously affecting the sensitivity. The latter depends on the formation of the yellow arsenomolybdate complex which requires a large excess of acid. In the experience of the author, variations of the blank value and serious disagreement between duplic...
متن کاملNature of the primary photochemical events in rhodopsin and bacteriorhodopsin.
II. Structure and function of rhodopsin and bacteriorhodopsin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 294 A. Organization of the proteins in the membrane . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 296 B. The photobleaching sequence of rhodopsin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 297 C. The photocycle of bact...
متن کاملSensory rhodopsin II and bacteriorhodopsin: light activated helix F movement.
EPR spectroscopy in combination with site directed spin labeling (SDSL) has become a valuable tool for structural investigations as well as for kinetic studies on proteins. This method has been especially useful for membrane proteins in yielding structural and functional data. This information is not easily available from other techniques, like, e.g., X-ray crystallography or electron microscop...
متن کاملConformations of the rhodopsin third cytoplasmic loop grafted onto bacteriorhodopsin.
BACKGROUND The third cytoplasmic loop of rhodopsin (Rho EF) is important in signal transduction from the retinal in rhodopsin to its G protein, transducin. This loop also interacts with rhodopsin kinase, which phosphorylates light-activated rhodopsin, and arrestin, which displaces transducin from light-activated phosphorylated rhodopsin. RESULTS We replaced eight residues of the EF loop of ba...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1981
ISSN: 0014-2956
DOI: 10.1111/j.1432-1033.1981.tb06345.x