Fluorescence studies of two γ-gliadin fractions from bread wheat

Two γ-gliadin fractions, designated γ_III and γ_V, were purified from cv. Chinese Spring and shown by N-terminal amino acid sequencing to be typical γ-gliadin types. Fluorescence spectroscopy of the gliadin fractions under non-denaturing conditions indicated that the tryptophan residues were exposed to the solvent. Under denaturing conditions only small changes were observed in fluorescence intensity and maximum emission wavelength, confirming that the tryptophan residues were exposed to the solvent prior to denaturation. Time-resolved fluorescence measurements gave rotational correlation times of 3-6 ns, indicating a high degree of mobility.