1968 年 32 巻 8 号 p. 988-994
The molecular conformation of the alkaline proteinase of Aspergillus sojae in aqueous solution was investigated by the optical rotatory dispersion, Cotton effects, infra-red absorption spectra (amide I and V bands), ultraviolet difference spectra, etc. It is concluded that; (1) there are about 10 to 15% of the α-helix and a small amount of the β-structure in the enzyme molecule, but most parts of the peptide chain are present as the disordered structure; (2) the enzyme molecule is compactly folded even in the disordered parts; and (3) the two tryptophan residues involved in the peptide chain are burried in the interior of the molecule.
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