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

Rapid formation of a molten globule intermediate in refolding of α-lactalbumin

https://ir.soken.ac.jp/records/4276
https://ir.soken.ac.jp/records/4276
9848fde7-3e48-4d58-8699-1611c52e3a0b
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-11
タイトル
タイトル Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
タイトル
タイトル Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
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 ARAI, Munehito

× ARAI, Munehito

ARAI, Munehito

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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 Backgound: The molten globule state is an intermediate between the native and the fully unfolded states of globular proteins and is purported to be an obligatory on-pathway intermediate of protein folding. The molten globule state of α-lactalbumin has been best characterized, but two major issues have yet to be clarified. At which stage of the kinetic refolding is the molten globule state stably organized? And what is the major driving force that stabilizes the molten globule state? We address these questions in this paper.

ResultsWe have investigated the refolding kinetics of α-lactalbumin using stopped-flow CD and fluorescence, acrylamide quenching and pulsed hydrogen exchange NMR techniques. A burst-phase intermediate was observed to form within 15 ms. The intermediate was characterized by pronounced, hydrogen-bonded secondary structure, exposure of hydrophobic surfaces and the absence of tertiary structure. Furthermore, the stability of the secondary structure is the same as that in the equilibrium molten globule state.

ConclusionThe burst-phase intermediate in α-lactalbumin refolding is identical with the molten globule state. Two different models, the hydrophobic collapse model and the secondary-structure coalescence model, of protein folding are discussed on the basis of the present results. The importance of solvent-separated hydrophobic interactions that stabilize the molten globule state is proposed.
書誌情報 Folding and Design
en : Folding and Design

巻 1, 号 4, p. 275-287, 発行日 1996-08
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 1359-0278
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/S1359-0278(96)00041-7
関連名称 10.1016/S1359-0278(96)00041-7
権利
権利情報 © 1996 Elsevier Ltd.
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