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

Chaperonin-Affected Folding of Globular Proteins

https://ir.soken.ac.jp/records/4305
https://ir.soken.ac.jp/records/4305
58e5488e-09e0-4d43-bf31-9c632f8a9ef4
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-17
タイトル
タイトル Chaperonin-Affected Folding of Globular Proteins
タイトル
言語 en
タイトル Chaperonin-Affected Folding of Globular Proteins
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

WEKO 2361

KUWAJIMA, Kunihiro

Search repository
TADASHI, Makio

× TADASHI, Makio

WEKO 2495

TADASHI, Makio

Search repository
INOBE, Tomonao

× INOBE, Tomonao

WEKO 2513

INOBE, Tomonao

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 studied the effect of GroEL on the kinetic refolding ofα-lactalbumin by stopped-flow fluorescence techniques. We usedwild-type GroEL and its ATPase-defficient mutant D398A, and studied thebinding constants between GroEL and the molten globule foldingintermediate at various concentrations of ADP and ATP. The results arecompared with titration of GroEL with the nucleotides, ADP, ATP-analogs(ATP-γS and AMP-PNP) and ATP, which have shown that bothADP and the ATP analogs are bound to GroEL in a non-cooperativemanner but that ATP shows a cooperative effect. Similarly, the bindingconstant between GroEL and the folding intermediate decreased in acooperative manner with an increase in ATP concentration although itshowed non-cooperative decrease with respect to ADP concentration. Itis shown that the allosteric control of GroEL by the nucleotides isresponsible for the above behavior of GroEL and that the observeddifference between the ATP- and ADP-induced transitions of GroEL isbrought about by a small difference in an allosteric parameter (the ratio ofthe nucleotide affinities of GroEL in the high-affinity and the low-affinitystates), i.e., 4.1 for ATP and 2.6 for ADP.
書誌情報 Journal of Biological Physics
en : Journal of Biological Physics

巻 28, 号 2, p. 77-93, 発行日 2002
出版者
出版者 SpringerLink
ISSN
収録物識別子タイプ ISSN
収録物識別子 0092-0606
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1023/A:1019993102869
関連名称 10.1023/A:1019993102869
権利
権利情報 SpringerLink(The original publication is available at www.springerlink.com)
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