Abstract
The secondary structure of γ1 globulin from rice embryo was investigated by means of optical rotatory dispersion, circular dichroism and infrared spectroscopy. The optical rotatory dispersion curve of the native γ1 globulin gave a trough at 233mμ with a [m']233 value of -2100°, and the Moffitt-Yang plot gave the parameters of a0=-237 and b0=-20. These data suggest the presence of 3% helix and 38% β structure in the molecule. Circular dichroism exhibits a negative extremum at 218mμ, giving a [θ]R value of -3730, which suggests the presence of 16% β structure. Infrared spectrum of_??_thin film of γ1 globulin showed absorption bands at 695 and 660cm-1 with a small hump at 615cm-1characteristic of the β structure, random coil and α helix, respectively. The protein in heavy water exhibits the absorption maximum at 1630cm-1, which is also characteristic of the β structure.
