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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/42769848fde7-3e48-4d58-8699-1611c52e3a0b
| 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× KUWAJIMA, Kunihiro |
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| 著者別名 |
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. |
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| 書誌情報 |
Folding and Design en : Folding and Design 巻 1, 号 4, p. 275-287, 発行日 1996-08 |
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| 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. | |||||
