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Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering
https://ir.soken.ac.jp/records/4314
https://ir.soken.ac.jp/records/431424851d30-df82-4fc5-ac91-c862c2885f49
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-19 | |||||
| タイトル | ||||||
| タイトル | Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering | |||||
| タイトル | ||||||
| タイトル | Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering | |||||
| 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× et, al. |
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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 measured the denaturation and reassembly of Escherichia coli chaperonin GroEL using small-angle solution X-ray scattering, which is a powerful technique for studying the overall structure and assembly of a protein in solution. The results of the urea-induced unfolding transition show that GroEL partially dissociates in the presence of more than 2 M urea, cooperatively unfolds at around 3 M urea, and is in a monomeric random coil-like unfolded structure at more than 3.2 M urea. Attempted refolding of the unfolded GroEL monomer by a simple dilution procedure is not successful, leading to formation of aggregates. However, the presence of ammonium sulfate and MgADP allows the fully unfolded GroEL to refold into a structure with the same hydrodynamic dimension, within experimental error, as that of the native GroEL. Moreover, the X-ray scattering profiles of the GroEL thus refolded and the native GroEL are coincident with each other, showing that the refolded GroEL has the same structure and the molecular mass as the native GroEL. These results demonstrate that the fully unfolded GroEL monomer can refold and reassemble into the native tetradecameric structure in the presence of ammonium sulfate and MgADP without ATP hydrolysis and preexisting chaperones. Therefore, GroEL can, in principle, fold and assemble into the native structure according to the intrinsic characteristic of its polypeptide chain, although preexisting GroEL would be important when the GroEL folding takes place under in vivo conditions, in order to avoid misfolding and aggregation. | |||||
| 書誌情報 |
Protein Science en : Protein Science 巻 12, 号 4, p. 672-680, 発行日 2003-04 |
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| 出版者 | ||||||
| 出版者 | Wiley | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0961-8368 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1110/ps.0233603 | |||||
| 関連名称 | 10.1110/ps.0233603 | |||||
| 権利 | ||||||
| 権利情報 | © 2003 The Protein Society | |||||
| フォーマット | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
