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

Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond

https://ir.soken.ac.jp/records/4282
https://ir.soken.ac.jp/records/4282
cc9bc9c1-fedd-4ffd-9add-574d08891e75
名前 / ファイル ライセンス アクション
5560070710_ftp.pdf 5560070710_ftp (2.2 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-11
タイトル
タイトル Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond
タイトル
言語 en
タイトル Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond
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
著者 IKEGUCHI, Masamichi

× IKEGUCHI, Masamichi

WEKO 2379

IKEGUCHI, Masamichi

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KATO, Masao

× KATO, Masao

WEKO 2498

KATO, Masao

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SUGAI, Shintaro

× SUGAI, Shintaro

WEKO 2363

SUGAI, Shintaro

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FUJINO, Motoaki

× FUJINO, Motoaki

WEKO 2405

FUJINO, Motoaki

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

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著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
抄録
内容記述タイプ Abstract
内容記述 The guanidine hydrochloride concentration dependence of the folding and unfolding rate constants of a derivative of α-lactalbumin, in which the 6-120 disulfide bond is selectively reduced and S-carboxymethylated, was measured and compared with that of disulfide-intact α-lactalbumin. The concentration dependence of the folding and unfolding rate constants was analyzed on the basis of the two alternative models, the intermediate-controlled folding model and the multiple-pathway folding model, that we had proposed previously. All of the data supported the multiple-pathway folding model. Therefore, the molten globule state that accumulates at an early stage of folding of α-lactalbumin is not an obligatory intermediate. The cleavage of the 6-120 disulfide bond resulted in acceleration of unfolding without changing the refolding rate, indicating that the loop closed by the 6-120 disulfide bond is unfolded in the transition state. It is theoretically shown that the chain entropy gain on removing the cross-link from a random coil chain with helical stretches can be comparable to that from an entirely random chain. Therefore, the present result is not inconsistent with the known structure in the molten globule intermediate. Based on this result and other knowledge obtained so far, the structure in the transition state of the folding reaction of α-lactalbumin is discussed.
書誌情報 Protein Science
en : Protein Science

巻 7, 号 7, p. 1564-1574, 発行日 1998-07
出版者
出版者 Wiley
ISSN
収録物識別子タイプ ISSN
収録物識別子 0961-8368
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 https://doi.org/10.1002/pro.5560070710
関連名称 10.1002/pro.5560070710
権利
権利情報 © 1998 The Protein Society
関連サイト
識別子タイプ URI
関連識別子 http://olabout.wiley.com/WileyCDA/Section/id-820227.html
関連名称 Copyright
フォーマット
内容記述タイプ Other
内容記述 application/pdf
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
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