| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2014-01-08 |
| タイトル |
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タイトル |
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozyme |
| タイトル |
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タイトル |
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozyme |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
metadata only access |
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アクセス権URI |
http://purl.org/coar/access_right/c_14cb |
| 著者 |
IKEGUCHI, Masamichi
KUWAJIMA, Kunihiro
MITANI, Masahiro
SUGAI, Shintaro
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| 著者別名 |
桑島, 邦博
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
The refolding kinetics of α-lactalbumin at different concentrations of guanidine hydrochloride have been investigated by means of kinetic circular dichroism and stopped-flow absorption measurements. The refolding reaction consists of at least two stages, the instantaneous accumulation of the transient intermediate that has peptide secondary structure and the subsequent slow process associated with formation of tertiary structure. The transient intermediate is compared with the well-characterized equilibrium intermediate observed during the denaturant-induced unfolding, (i) Stabilities of the secondary structures against the denaturant, (ii) affinities for Ca2+, and (iii) tryptophan absorption properties of the transient and equilibrium intermediates were investigated. In all of these respects, the transient intermediate is identical with the equilibrium one, demonstrating the validity of the use of the equilibrium intermediate as a model of the folding intermediate. Essentially the same transient intermediate was also detected in the folding of lysozyme, the protein known to be homologous to α-lactalbumin but whose equilibrium unfolding is represented as a two-state reaction. The stability and cooperativity of the secondary structure of the intermediate of lysozyme are compared with those of α-lactalbumin. The results show that the protein folding occurring via the intermediate is not limited to the proteins that show equilibrium intermediates. Although the unfolding equilibria of most proteins are well approximated as a two-state reaction, the two-state hypothesis may not be applicable to the folding reaction under the native condition. Two models of protein folding, intermediate-controlled folding model and multiple-pathway folding model, which are different in view of the role of the intermediate in determining the pathway of folding, are also discussed. |
| 書誌情報 |
Biochemistry
en : Biochemistry
巻 25,
号 22,
p. 6965-6972,
発行日 1986
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| 出版者 |
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出版者 |
American Chemical Society |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
00062960 |
| PubMed番号 |
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識別子タイプ |
PMID |
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関連識別子 |
3801404 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
http://doi.org/10.1021/bi00370a034 |
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関連名称 |
10.1021/bi00370a034 |
| 権利 |
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権利情報 |
© 1986 American Chemical Society |
