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- W1799572558 abstract "This chapter discusses the late photoproducts and signaling states of bovine rhodopsin. Rhodopsin is an integral membrane protein of the disc membrane stacks filling the rod outer segment. By its lipid composition (which includes large amounts of polyunsaturated fatty acids), the disc membrane is extremely fluid. This property is crucially important for signal transduction, because it favors both the formation of rhodopsin's active state and the rapid lateral and rotational diffusion of the receptor, thus providing opportunities for collisional coupling in the random walk amplifier mechanism. Bovine rhodopsin, is 348 amino acid residues in length, identical to human rhodopsin at all but 23 positions. The disposition of the helical transmembrane stretches became best visible by cryo-electron microscopy of two-dimensional crystals of frog rhodopsin. The evidence for conformational changes, related to photoproduct formation is discussed. It is seen that the Meta photointermediates and the structural alterations behind them play a major role in the proteinprotein interactions underlying signal transduction. They serve as a model for light-independent signaling by the apoprotein opsin and its reversible complexes with the photolyzed chromophore. The G-protein, rhodopsin kinase, and arrestin are discussed in the chapter for both modes of signaling." @default.
- W1799572558 created "2016-06-24" @default.
- W1799572558 creator A5021314496 @default.
- W1799572558 date "2000-01-01" @default.
- W1799572558 modified "2023-10-15" @default.
- W1799572558 title "Chapter 3 Late photoproducts and signaling states of bovine rhodopsin" @default.
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