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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/4282cc9bc9c1-fedd-4ffd-9add-574d08891e75
名前 / ファイル | ライセンス | アクション |
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5560070710_ftp (2.2 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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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 | ||||||
タイトル | Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond | |||||
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 | |||||
著者 |
IKEGUCHI, Masamichi
× IKEGUCHI, Masamichi× KATO, Masao× SUGAI, Shintaro× FUJINO, Motoaki× KUWAJIMA, Kunihiro |
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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 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 |
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出版者 | ||||||
出版者 | Wiley | |||||
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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 | |||||
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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 | |||||
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内容記述タイプ | Other | |||||
内容記述 | application/pdf | |||||
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出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |