Structure of Aggregates Formed by a Thermally Denatured Protein after Quench

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  • KONDO Aiko
    Department of Macromolecular Science, Osaka University
  • SATO Takahiro
    Department of Macromolecular Science, Osaka University

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  • 熱変性タンパク質の冷却に伴い形成される会合体の構造
  • ネツ ヘンセイ タンパクシツ ノ レイキャク ニ トモナイ ケイセイサレル カイゴウタイ ノ コウゾウ

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Abstract

We have investigated the structure of aggregates formed by thermally denatured β-lactoglobulin in 0.1 M aqueous NaCl after quench at pH=7 and at a protein concentration ~10-3 g/cm3, using size exclusion chromatography equipped with a multi-angle light scattering detector (SEC-MALS), circular dichroism, and viscometry. While circular dichroism indicated an irreversible thermal denaturation of β-lactoglobulin in that solvent, viscometry demonstrated that β-lactoglobulin takes a random coil conformation upon heating and a compact one upon cooling. SEC-MALS results indicated that quenched β-lactoglobulin after denaturation exists as two kinds of aggregates in aqueous solution. From the molar mass obtained, we conclude that the major smaller aggregate comprises five β-lactoglobulin chains on average, and takes a compact conformation. The molar mass dependence of the radius of gyration for the larger aggregate was explained by the branched touched-bead model where the bead diameter was assumed to be the same as that of the smaller aggregate or the single protein molecule.<br>

Journal

  • KOBUNSHI RONBUNSHU

    KOBUNSHI RONBUNSHU 64 (7), 452-457, 2007

    The Society of Polymer Science, Japan

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