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Abstract
The conformational change of the 11S component of soybean proteins in acid was measured by ultraviolet difference spectra, optical rotatory dispersion and circular dichroism. Below pH 4, the change of tertiary structure that the tyrosine residues were exposed and the tryptophan residues were barried into the molecule was recognized, and, between pH 2 and 0.64, the change was attained to maximum. The secondary structure, β-structure, of the 11S component was almost stable at pH 1.22.
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