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- W2020105274 abstract "Squid retinochrome and its photoproduct (P465) are optically active, indicating that both all-trans and 11-cis retinal become asymmetric upon binding to the retinochrome protein. The protein exhibits a CD spectrum in the far ultraviolet region characteristic of an α-helix conformation. The positive CD bands in the visible region are attributable to the chromophore retinal, and the large negative CD bands at 305 nm and 275 nm are ascribed to residues such as Tyr, Trp and Cys in the protein moiety. On the liberation of retinal from the protein the CD band in the visible range disappears completely and those in the near ultraviolet range decrease remarkably in magnitude. These facts suggest that the chromophore retinal and residues such as Tyr, Trp and Cys in the protein moiety are restricted in free rotation by the binding of the chromophore with retinochrome protein. On the basis of the above results the mechanism of induction of the CD of retinal is discussed." @default.
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- W2020105274 date "1974-05-01" @default.
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- W2020105274 title "Circular dichroism of squid retinochrome" @default.
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- W2020105274 doi "https://doi.org/10.1016/0005-2795(74)90072-5" @default.
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