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Chaperonin-Affected Folding of Globular Proteins
https://ir.soken.ac.jp/records/4305
https://ir.soken.ac.jp/records/430558e5488e-09e0-4d43-bf31-9c632f8a9ef4
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-17 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Chaperonin-Affected Folding of Globular Proteins | |||||||||||
| タイトル | ||||||||||||
| タイトル | Chaperonin-Affected Folding of Globular Proteins | |||||||||||
| 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
× TADASHI, Makio
× INOBE, Tomonao
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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 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 |
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| 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) | |||||||||||
