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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/4316501c53aa-2ac9-4029-bfcf-c08be61b5572
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 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
× SAEKI, Kimiko
× 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 | 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 |
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| 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. | |||||||||||
