The Structural Environment of the Tryptophanyl Residue of Horse Heart Ferricytochrome c
作者： Earle Stellwagen , Susan Van Rooyan
DOI: 10.1016/S0021-9258(18)99527-X
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摘要: 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 the 4 residues are iodinated by reaction protein with potassium triiodide. These results indicate located on surface. Treatment N-bromosuccinimide oxidizes residue both methionyl Changes reduced viscosity, ionization phenolic hydroxyl groups, visible absorbance spectrum, exposure heme moiety oxidation buried due a partial unfolding native conformation c.
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