The Effect of Reduction of The Disulphide Bond on the Fluorescence of High-Sulphur Wool Proteins

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Abstract
Reduction of the disulphide bonds affects the fluorescence emission from many proteins; this change is generally correlated with a change in the protein conformation (Cowgill 1964, 1966; Stryer, Holmgren, and Reichard 1967). Cowgill (1967) has reported the quenching effect of disulphide and thiol groups on the tryptophan and tyrosine fluorescence from model peptides when the quenching moiety is present in the same molecule as the chromophore. Similar observations have been made in this laboratory using a high-sulphur fraction extracted from wool protein.

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