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A folding model of α-lactalbumin deduced from the three-state denaturation mechanism
https://ir.soken.ac.jp/records/4117
https://ir.soken.ac.jp/records/4117b2f3338e-0132-4b81-a6b2-953168735944
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
|---|---|---|---|---|---|---|---|---|
| 公開日 | 2013-12-24 | |||||||
| タイトル | ||||||||
| タイトル | A folding model of α-lactalbumin deduced from the three-state denaturation mechanism | |||||||
| タイトル | ||||||||
| タイトル | A folding model of α-lactalbumin deduced from the three-state denaturation mechanism | |||||||
| 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 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro
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| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | It has been shown that α-lactalbumin undergoes a three-state denaturation, involving a helical intermediate state, on treatment with guanidine hydrochloride. The unfolding of the protein and the characteristics of the intermediate state are examined by means of circular dichroism, difference spectra and pH-jump measurements to investigate the temperature dependence and kinetic properties of the unfolding and refolding, the pH dependence of the transition between the intermediate and the fully unfolded states, and the effect of disulphide bond reduction on the stabilization of the intermediate. The results show that the long-range specific interactions such as specific electrostatic interactions and disulphide linkages are not important for stabilizing the intermediate, and that the transition between the intermediate and the fully unfolded states is extremely rapid (a relaxation time of less than one millisecond) and may correspond to the helix-coil transition of a polypeptide backbone. On the other hand, the activation parameters of the transition between the native and the intermediate states have suggested that the final stabilization by charge-pair interactions is preceded by hydrophobic interactions in the process of going from the intermediate to the native state. The mechanism of folding of the protein is discussed, and the folding process from the fully unfolded to the native state is apparently divided into at least three main steps: (1) the formation of incipient helical structures dictated by local interactions; (2) the packing of the helical segments accompanied with hydrophobic interactions; (3) the final stabilization by the electrostatic interactions. The relevance to the current theoretical results on protein folding is also discussed. |
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| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 114, 号 2, p. 241-258, 発行日 1977-08-05 |
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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 | 0022-2836 | |||||||
| DOI | ||||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | https://doi.org/10.1016/0022-2836(77)90208-X | |||||||
| 関連名称 | 10.1016/0022-2836(77)90208-X | |||||||
| 権利 | ||||||||
| 権利情報 | © 1977 Published by Elsevier Ltd. | |||||||
