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Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix
https://ir.soken.ac.jp/records/4297
https://ir.soken.ac.jp/records/4297f89b5df2-d2a9-442c-9f59-36640cf20da4
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 公開日 | 2014-03-14 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix | |||||||||||
| タイトル | ||||||||||||
| タイトル | Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix | |||||||||||
| 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 |
FORGE, Vincent
× FORGE, Vincent
× 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 | The refolding of β-lactoglobulin, a β-barrel protein consisting of β strands βA-βI and one major helix, is unusual because non-native α-helices are formed at the beginning of the process. We studied the refolding kinetics of bovine β-lactoglobulin A at pH 3 using the stopped-flow circular dichroism and manual H/2H exchange pulse labeling coupled with heteronuclear NMR. The protection pattern from the H/2H exchange of the native state indicated the presence of a stable hydrophobic core consisting of βF, βG and βH strands. The protection pattern of the kinetic intermediate obtained about one second after initiating the reaction was compared with that of the native state. In this relatively late kinetic intermediate, which still contains some non-native helical structure, the disulfide-bonded β-hairpin made up of βG and βH strands was formed, but the rest of the molecule was fluctuating, where the non-native α-helices may reside. Subsequently, the core β-sheet extends, accompanied by a further α-helix to β-sheet transition. Thus, the refolding of β-lactoglobulin exhibits two elements: the critical role of the core β-sheet is consistent with the hierarchic mechanism, whereas the α-helix to β-sheet transition suggests the non-hierarchic mechanism. | |||||||||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 296, 号 4, p. 1039-1051, 発行日 2000-03-03 |
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| 出版者 | ||||||||||||
| 出版者 | Elsevier | |||||||||||
| 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/10.1006/jmbi.1999.3515 | |||||||||||
| 関連名称 | 10.1006/jmbi.1999.3515 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2000 Academic Press | |||||||||||
