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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

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/4314
24851d30-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
言語 en
タイトル Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering
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

WEKO 2491

ARAI, Munehito

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

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et, al.

× et, al.

WEKO 3119

et, al.

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
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
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
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