Abstract
The effect of temp. on soybean glycinin in 8M urea or 6M guanidine hydrochloride solution was studied by circular dichroism and optical rotatory dispersion measurements. At room temp. the protein assumes an unordered conformation in the presence of the denaturant. With increase in temp., mean residue ellipticity in the range 250-210 nm assumes more negative values, suggesting formation of ordered conformations at higher temperatures.
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