Abstract
The effect of SDS on conformation of glycinin from soybean (Glycine max) was studied by the techniques of optical rotatory disperion (ORD), circular dichroism (CD), fluorescence spectrophotometry, and viscosity measurements. The addition of SDS decreased the intensity of bands in the near-UV-CD spectrum of the protein, suggesting disruption of the tertiary structure. In the far-UV-CD spectrum the ellipticity values increased. Calculation of the alpha-helical content of the protein showed that it increased with increasing SDS concn. This conclusion was supported by difference CD spectra, ORD, and fluorescence spectral data. Reduced viscosity of the protein did not change significantly with increases in SDS concn., indicating slight changes in hydrodynamic vol. of the protein.
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