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

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/4297
f89b5df2-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

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FORGE, Vincent

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

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 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
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
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