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- W1980702225 abstract "Quenching of Tryptophan Fluorescence in Skeletal Myosin RodYoke-chen Chang and Richard D. LudescherDepartment of Food Science, Rutgers UniversityNew Brunswick, NJ 08903ABSTRACTThe fibrous region of myosin, called myosin rod when isolated from myosinafter proteolysis, is a two—stranded coiled—coil made up of identical chains ofnearly 1000 residues. Myosin from rabbit skeletal muscle has two tryptophansper chain located at identical hydrophobic d sites in the heptad repeat whichforms the basis for hydrophobic dimerization. Steady-state quenching of thesetryptophans by KI shows downward curvature in a classic Stern-Volmer plot; analysisusing a modified S-V equation indicates that only about 80% of the tryptophans areaccessible to this charged quencher. The emission intensity decays are complex andare fit to lifetimes of 5.3, 1.6 and 0.4 ns with relative amplitudes of 0.78, 0.13,and 0.09. Lifetime resolved quenching studies indicate that only the long lifetimecomponent is quenched by iodide; the collisional rate constant for quenching thiscomponent is very similar to that calculated from the steady—state quenching data.The long lifetime component thus corresponds to a population of solvent accessibletryptophans that may be on the surface of the coiled-coil protein. These studiessuggest that the tryptophans in myosin rod may be in equilibrium between accessibleand inaccessible sites at the coiled—coil interface." @default.
- W1980702225 created "2016-06-24" @default.
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- W1980702225 date "1992-04-01" @default.
- W1980702225 modified "2023-09-23" @default.
- W1980702225 title "<title>Quenching of tryptophan fluorescence in skeletal myosin rod</title>" @default.
- W1980702225 doi "https://doi.org/10.1117/12.58210" @default.
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