Stopped-flow small-angle X-ray scattering study on the acid-denaturation of Taka-amylase A.

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概要

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• A stopped-flow small-angle X-ray scattering method was applied to study the structural change of Taka-amylase A by acid-denaturation. The structural change could be described by two successive steps. The first step is described by a change in the eccentricity of a prolate ellipsoid from 2.0 to 2.4; this was estimated by a comparison between the observed scattering profile and the theoretical scattering function of the prolate ellipsoid. The second step supposes that the X-ray scatterer in a solution comprises two kinds of particles with large and small radii of gyration. The X-ray scatterer with a large radius expands with time. By contrast, the radius of gyration of the small scatterer corresponds to that of a native Taka-amylase A monomer and it remains unchanged. These facts imply that in the denaturation of Taka-amylase A the molecule is prolonged by a partial unfolding of the polypeptide chain and then aggregates with each other.

• 公益社団法人 日本化学会の論文

著者

• SATO Mamoru

  Institute for Protein Research, Osaka University

• Hata Yasuo

  Institute For Chemical Research Kyoto University

• Katsube Yukiteru

  Institute For Protein Research Osaka University

• Kasai Nobutami

  Department Of Applied Biological Science Tokyo University Of Science

• Tanaka Nobuo

  Institute For Solid State Physics University Of Tokyo

• Kato Mitsunori

  Department of Applied Chemistry, Faculty of Engineering, Osaka University

• Hozaki Tatsuya

  Department of Applied Chemistry, Faculty of Engineering, Osaka University

• Morimoto Yukio

  Institute for Protein Research

• Hata Yasuo

  Institute for Protein Research

• Sato Mamoru

  Institute for Protein Research

• Katsube Yukiteru

  Institute for Protein Research

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