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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL

https://ir.soken.ac.jp/records/4272
https://ir.soken.ac.jp/records/4272
5609a049-fc4b-46b9-a8b7-90a5af0efb21
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-10
タイトル
タイトル Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL
タイトル
タイトル Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 KATSUMATA, Kumiko

× KATSUMATA, Kumiko

KATSUMATA, Kumiko

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OKAZAKI, Akira

× OKAZAKI, Akira

OKAZAKI, Akira

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TSURUPA, Galina P

× TSURUPA, Galina P

TSURUPA, Galina P

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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著者別名 桑島, 邦博

× 桑島, 邦博

桑島, 邦博

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抄録
内容記述タイプ Abstract
内容記述 GroEL is known to retard the refolding of apo-α-lactalbumin by interacting with the molten globule state of the protein. In order to investigate the dominant forces in this interaction, the GroEL-affected kinetic refolding of apo-α-lactalbumin from its acidic molten globule state was studied at different temperatures and in the presence of different kinds of monovalent cations at a fixed temperature (25°C), by stopped-flow fluorescence measurements. The binding constant between GroEL and α-lactalbumin in the molten globule state was evaluated quantitatively from the kinetic refolding curves in the absence and presence of GroEL. The binding was found to be entropy-driven at room temperature and the heat capacity change for the binding was found to be largely negative (−3.6 kJ mol−1·K−1), indicating that GroEL binds to α-lactalbumin through hydrophobic interactions. The study of the effect of different monovalent cations at various ionic strengths shows that the binding is strengthened by electrostatic screening by ions, demonstrating the importance of electrostatic interactions. The relationship of these results with a putative target recognition site of GroEL will be discussed.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 264, 号 4, p. 643-649, 発行日 1996-12-13
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 0022-2836
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1006/jmbi.1996.0666
関連名称 10.1006/jmbi.1996.0666
権利
権利情報 © 1996 Academic Press
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