Abstract
The circular dichroic spectra of α-globulin fromSesamum indicum L. was recorded in the presence of cetyltrimethyl ammonium bromide, Triton X-100 and Brij-36T. The protein in 0.2 M phosphate buffer pH 7.4 had about 25% Β-structure and 5% α-helix, the rest being aperiodic or irregular structure and a-helix, structure was increased by cationic detergent cetyl trimethyl ammonium bromide. But, the increase in α-helix content was much less than that induced by an anionic detergent, sodium dodecyl sulphate. In non-ionic detergent like Brij-36T and Triton X-100, specific Β-structures like II-Β and I-Β were formed along with changes in α-helical and aperiodic structures. These results suggest that the protein has a fairly labile quaternary structure.
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