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- W1567118861 startingPage "4801" @default.
- W1567118861 abstract "Abstract The ultraviolet solvent perturbation difference spectrum of horse heart ferricytochrome c in 20% ethylene glycol is equivalent to that calculated for 2 tyrosyl and no tryptophanyl residues. Two of the 4 tyrosyl residues are iodinated by reaction of the protein with potassium triiodide. These results indicate that 2 of the tyrosyl residues of ferricytochrome c are located on the protein surface. Treatment of the protein with N-bromosuccinimide oxidizes the tryptophanyl residue and both methionyl residues. Changes in the reduced viscosity, ionization of the phenolic hydroxyl groups, visible absorbance spectrum, and exposure of the heme moiety indicate that oxidation of the tryptophanyl residue and the buried methionyl residue is due to a partial unfolding of the native conformation of ferricytochrome c." @default.
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- W1567118861 date "1967-10-01" @default.
- W1567118861 modified "2023-10-15" @default.
- W1567118861 title "The Structural Environment of the Tryptophanyl Residue of Horse Heart Ferricytochrome c" @default.
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- W1567118861 doi "https://doi.org/10.1016/s0021-9258(18)99527-x" @default.
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