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- W2010144515 abstract "Oxidation with N-bromosuccinimide detects a total of about ten tryptophan residues in detergent-solubilized bovine rhodopsin. One of these tryptophans is more reactive in bleached than in unbleached rhodopsin, suggesting its involvement in the chromophore binding site. Oxidation of this residue is accompanied by loss of the 500nm. absorbance in unbleached rhodopsin. Similar experiments with bacteriorhodopsin are inconclusive." @default.
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- W2010144515 title "Reactivity of tryptophans in rhodopsin" @default.
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- W2010144515 doi "https://doi.org/10.1016/0006-291x(76)90026-7" @default.
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