Rhodopsin and G-protein Linked Receptors by A.G. Lee (Eds.)

Rhodopsin and G-protein Linked Receptors by A.G. Lee (Eds.)

By A.G. Lee (Eds.)

The amount of data to be had approximately membrane proteins is now too huge for anyone individual to be acquainted with something yet a truly small a part of the first literature. a chain of volumes focusing on molecular points of organic membranes as a result turns out well timed. The wish is that, while entire, those volumes will supply a handy creation to the examine of a variety of membrane services. program of the innovations of molecular biology has supplied the sequences of a really huge variety of membrane proteins, and has ended in the invention of superfamilies of membrane proteins of comparable constitution. The vintage instance of the superfamily is the seven helix receptor superfamily, all similar in constitution to bacteriorhodpsin, and named after the seven trans-membrane a-helices pointed out in bacteriorhodpsin. This quantity explores the buildings and capabilities of this great relations.

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Additional resources for Rhodopsin and G-protein Linked Receptors

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Biol. Chem. 254, 4653-4660. Mone, A. , & Litman, B. J. (1990). Cholesterol increases the stability of rhodopsin in egg PC vesicles to thermally induced unfolding. Biophys. J. 57, 74a. Mone, A. , & Litman, B. J. (1991). Variation of phospholipid headgroup composition modulates the formation of metarhodopsin II. Biophys. J. 59, 621 a. Monger, T. , Alfano, R. , & Callender, R. H. (1979). Photochemistry ofrhodopsin and isorhodopsin investigated on a picosecond time scale. Biophys. J. 27, 105-115. Mouritsen, O.

80 A. Photorhodopsin . . . . . . . . . . . . . . . . 82 B. Bathorhodopsin . . . . . . . . . . . . . . . . 84 C. Ultrafast Spectroscopic Studies . . . . . . . . . . . . 88 D. Quantum Efficiency of the Primary Event . . . . . . . . . 96 E. Molecular Dynamics of the Primary Event . . . . . . . . . 98 F. Energy Storage in the Primary Event . . . . . . . . . . 103 G. Molecular Origins of Photoreceptor Noise . . . . . . .

2. C~(~) ,k~~ ,~ ,~ AI,~) ,~ ...... e.. ~ . ':----~[ ~ ........ , ~ ..... ~1~ ~ ........ ~ ~_,~' ..... ~ '" ,~o® ~ " " ~®©(E~"~" Figure 4. Amino acid sequence, and putative membrane spanning regions of human rhodopsin. Amino acid abbreviations are as given in Figure 1. The chromophore is covalently linked to the protein via a protonated Schiff base linkage to Lys296. teristic of nearly all biological signal transduction systems. Until recently, bacteriorhodopsin's similarity to this family of proteins, and to rhodopsin in particular, seemed to be purely coincidental.

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