Abstract
Conformations of gluten, glutenin, and gliadin were studied by optical rotatory dispersion in 3 M urea plus 0.11 M KCl plus 0.02 M buffer at several pH values, and in 0.002 N HCl. Wavelength ranged from 600 to around 220 mμ or lower. A significant negative Cotton effect at 233 mμ was observed for each protein in all solvents studied. Values of b 0 from Moffit-Yang plots were interpreted conventionally ( b 0 = −630 for 100% right-handed α-helix). Optical rotatory dispersion data were also treated by a modified two-term Drude equation according to the method of Shechter and Blout. The results indicate that gliadin contains more α-helix than glutenin and that all three proteins contain more α-helix in hydrochloric acid than in urea solutions. Glutenin and gliadin are probably mixtures of random coil and helix.
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