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Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra
https://ir.soken.ac.jp/records/4145
https://ir.soken.ac.jp/records/4145235a5a19-cd98-4aae-b5a8-07e32aa648d4
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-01-15 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra | |||||||||||
| タイトル | ||||||||||||
| タイトル | Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra | |||||||||||
| 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 |
SUGAWARA, Tatsuro
× SUGAWARA, Tatsuro
× KUWAJIMA, Kunihiro
× 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 urea-induced unfolding of staphylococcal nuclease A has been studied by circular dichroism both at equilibrium and by the kinetics of unfolding and refolding (pH 7.0 and 4.5 °C), as a function of Ca2+ and thymidine 3′,5′-diphosphate (pdTp) concentration. The results are as follows. (1) The unfolding transition is shifted to higher concentrations of urea by Ca2+ and pdTp, and the presence of both ligands further stabilizes the protein. (2) In the first stage of kinetic refolding, the peptide ellipticity changes rapidly within the dead time of stopped-flow measurement (15 ms), indicating accumulation of a transient intermediate. This intermediate is remarkably less stable than those of other globular proteins previously studied. (3) Dependence of the folding and unfolding rate constants on urea concentration indicates that the critical activated state of folding ("transition state") has considerable structural organization. The transition state does not, however, have the capacity to bind Ca2+ and pdTp, as indicated by the effects of these ligands on the unfolding rate constant. (4) There are at least four different phases in the refolding kinetics in native conditions below 1 M urea. In the absence of pdTp, there are two phases in unfolding, while in the presence of pdTp the unfolding kinetics show a single phase. Some characteristics of the transient intermediate and of the transition state for folding are discussed. | |||||||||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 30, 号 10, p. 2698-2706, 発行日 1991-03 |
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| 出版者 | ||||||||||||
| 出版者 | American Chemical Society | |||||||||||
| ISSN | ||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||
| 収録物識別子 | 00062960 | |||||||||||
| PubMed番号 | ||||||||||||
| 識別子タイプ | PMID | |||||||||||
| 関連識別子 | 2001357 | |||||||||||
| DOI | ||||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | http://doi.org/10.1021/bi00224a018 | |||||||||||
| 関連名称 | 10.1021/bi00224a018 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 1991 American Chemical Society | |||||||||||
