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Unification of the folding mechanisms of non-two-state and two-state proteins.
https://ir.soken.ac.jp/records/4317
https://ir.soken.ac.jp/records/431763b7fcd5-0268-407e-9cea-0437e9f98ee5
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-19 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Unification of the folding mechanisms of non-two-state and two-state proteins. | |||||||||||
| タイトル | ||||||||||||
| タイトル | Unification of the folding mechanisms of non-two-state and two-state proteins. | |||||||||||
| 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 |
KAMAGATA, Kiyoto
× KAMAGATA, Kiyoto
× 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 | We have collected the kinetic folding data for non-two-state and two-state globular proteins reported in the literature, and investigated the relationships between the folding kinetics and the native three-dimensional structure of these proteins. The rate constants of formation of both the intermediate and the native state of non-two-state folders were found to be significantly correlated with protein chain length and native backbone topology, which is represented by the absolute contact order and sequence-distant native pairs. The folding rate of two-state folders, which is known to be correlated with the native backbone topology, apparently does not correlate significantly with protein chain length. On the basis of a comparison of the folding rates of the non-two-state and two-state folders, it was found that they are similarly dependent on the parameters that reflect the native backbone topology. This suggests that the mechanisms behind non-two-state and two-state folding are essentially identical. The present results lead us to propose a unified mechanism of protein folding, in which folding occurs in a hierarchical manner, reflecting the hierarchy of the native three-dimensional structure, as embodied in the case of non-two-state folding with an accumulation of the intermediate. Apparently, two-state folding is merely a simplified version of hierarchical folding caused either by an alteration in the rate-limiting step of folding or by destabilization of the intermediate. | |||||||||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 339, 号 4, p. 951-965, 発行日 2004-06-11 |
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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/j.jmb.2004.04.015 | |||||||||||
| 関連名称 | 10.1016/j.jmb.2004.04.015 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2004 Elsevier Ltd. | |||||||||||
