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

Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding

https://ir.soken.ac.jp/records/4316
https://ir.soken.ac.jp/records/4316
501c53aa-2ac9-4029-bfcf-c08be61b5572
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 Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding
タイトル
タイトル Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding
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 SAEKI, Kimiko

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SAEKI, Kimiko

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KUWAJIMA, Kunihiro

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KUWAJIMA, Kunihiro

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et, al.

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et, al.

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著者別名 桑島, 邦博

× 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 To investigate whether the structure partially formed in the molten globule folding intermediate of goat α-lactalbumin is further organized in the transition state of folding, we constructed a number of mutant proteins and performed Φ-value analysis on them. For this purpose, we measured the equilibrium unfolding transitions and kinetic refolding and unfolding reactions of the mutants using equilibrium and stopped-flow kinetic circular dichroism techniques. The results show that the mutants with mutations located in the A-helix (V8A, L12A), the B-helix (V27A), the β-domain (L52A, W60A), the C-helix (K93A, L96A), the C–D loop (Y103F), the D-helix (L105A, L110A), and the C-terminal 310-helix (W118F), have low Φ-values, less than 0.2. On the other hand, D87N, which is located on the Ca2+-binding site, has a high Φ-value, 0.91, indicating that tight packing of the side-chain around Asp87 occurs in the transition state. One β-domain mutant (I55V) and three C-helix mutants (I89V, V90A, and I95V) demonstrated intermediate Φ-values, between 0.4 and 0.7. These results indicate that the folding nucleus in the transition state of goat α-LA is not extensively distributed over the α-domain of the protein, but very localized in a region that contains the Ca2+-binding site and the interface between the C-helix and the β-domain. This is apparently in contrast with the fact that the molten globule state of α-lactalbumin has a partially formed structure inside the α-domain. It is concluded that the specific docking of the α and β-domains at a domain interface is necessary for this protein to organize its native structure from the molten globule intermediate.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 341, 号 2, p. 589-604, 発行日 2004-08-06
出版者
出版者 Elsevier
Online ISSN
収録物識別子タイプ ISSN
収録物識別子 0022-2836
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.jmb.2004.06.010
関連名称 10.1016/j.jmb.2004.06.010
権利
権利情報 © 2004 Elsevier Ltd.
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