| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2014-03-14 |
| タイトル |
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タイトル |
Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster |
| タイトル |
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タイトル |
Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster |
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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 |
IKURA, Teikichi
HAYANO, Toshiya
TAKAHASHI, Nobuhiro
KUWAJIMA, Kunihiro
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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 |
Escherichia coli cyclophilin A, a 164 residue globular protein, shows fast and slow phases of refolding kinetics from the urea-induced unfolded state at pH 7.0. Given that the slow phases are independent of the denaturant concentration and may be rate-limited by cis/trans isomerizations of prolyl peptide bonds, the fast phase represents the true folding reaction. The extrapolation of the fast-phase rate constant to 0 M urea indicates that the folding reaction of cyclophilin A is extraordinarily fast and has about 700 s−1 of the rate constant. Interrupted refolding experiments showed that the protein molecules formed in the fast phase had already been fully folded to the native state. This finding overthrows the accepted view that the fast folding is observed only in small proteins of fewer than 100 amino acid residues. Examination of the X-ray structure of cyclophilin A has shown that this protein has only one unique hydrophobic core (phenylalanine cluster) formed by evolutionarily conserved phenylalanine residues, and suggests that this architecture of the molecule may be responsible for the fast folding behavior. |
| 書誌情報 |
Journal of Molecular Biology
en : Journal of Molecular Biology
巻 297,
号 3,
p. 791-802,
発行日 2000-03-31
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| 出版者 |
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出版者 |
Elsevier |
| 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 |
0022-2836 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1006/jmbi.2000.3580 |
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関連名称 |
10.1006/jmbi.2000.3580 |
| 権利 |
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権利情報 |
© 2000 Academic Press |
