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Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of α-lactalbumin
https://ir.soken.ac.jp/records/4140
https://ir.soken.ac.jp/records/4140177cf1d3-6c2a-462e-a96c-8af13b405ba7
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-01-09 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of α-lactalbumin | |||||||||||
| タイトル | ||||||||||||
| タイトル | Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics 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 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro
× MITANI, Masahiro
× SUGAI, Shintaro
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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 | The reversible unfolding and refolding kinetics of α-lactalbumin induced by concentration jump of guanidine hydrochloride were measured at pH 7.0 and 25 °C using tryptophan absorption at 292 nm, with varying concentrations of the denaturant and free Ca2+. The refolding reaction of α-lactalbumin from the fully unfolded (D) state occurs through the two stages: (1) instantaneous formation of a compact intermediate (the A state) that has a native-like secondary structure; (2) tight packing of the preformed secondary structure segments to lead finally to the native structure, this stage being the rate-determining step of the reaction and associated with aquisition of the specific structure necessary for strong Ca2+ binding. Under strongly native conditions, the observed kinetics of refolding is also complicated by the presence of a slow-folding species (10%) in the unfolded state. Considering these facts, the microscopic rate constants in folding and unfolding directions have been evaluated from the observed kinetics and from the equilibrium constants of the transitions among the native (N), A and D states. Close linear relationships have been found in the plots of the activation free energies, obtained from the microscopic rate constants, against the denaturant concentration. They are similar to the linear relationship between the free energy of unfolding and the denaturant concentration. It was demonstrated that the slope of the plots should be approximately proportional to a change in accessible surface area of the protein during the respective activation process, and that only a third of the difference in accessible surface area between A and N is buried in the critical activated state of folding. However, the selective effect of Ca2+ binding on the folding rate constant has been observed also, demonstrating that the specific Ca2+-binding substructure in the N state is already organized in the activated state. Thus, only a part of the protein molecule involving the Ca2+-binding region is organized in the activated state, with the other part of the molecule being left less organized, suggesting that the second stage of folding may be a sequential growing process of organized assemblage of the preformed secondary structure segments. |
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| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 206, 号 3, p. 547-561, 発行日 1989-04-05 |
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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 | |||||||||||
| PubMed番号 | ||||||||||||
| 識別子タイプ | PMID | |||||||||||
| 関連識別子 | 2716061 | |||||||||||
| DOI | ||||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | https://doi.org/10.1016/0022-2836(89)90500-7 | |||||||||||
| 関連名称 | 10.1016/0022-2836(89)90500-7 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 1989 Published by Elsevier Ltd. | |||||||||||
