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The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
https://ir.soken.ac.jp/records/4329
https://ir.soken.ac.jp/records/43295ff789c7-9ad2-4323-857a-47598200e706
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-25 | |||||||||||
| タイトル | ||||||||||||
| タイトル | The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein | |||||||||||
| タイトル | ||||||||||||
| タイトル | The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein | |||||||||||
| 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 |
ENOKI, Sawako
× ENOKI, Sawako
× KUWAJIMA, Kunihiro
× et, al.
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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 | Folding mechanisms of a variant of green fluorescent protein (F99S/M153T/V163A) were investigated by a wide variety of spectroscopic techniques. Equilibrium measurements on acid-induced denaturation of the protein monitored by chromophore and tryptophan fluorescence and small-angle X-ray scattering revealed that this protein accumulates at least two equilibrium intermediates, a native-like intermediate and an unfolding intermediate, the latter of which exhibits the characteristics of the molten globule state under moderately denaturing conditions at pH 4. To elucidate the role of the equilibrium unfolding intermediate in folding, a series of kinetic refolding experiments with various combinations of initial and final pH values, including pH 7.5 (the native condition), pH 4.0 (the moderately denaturing condition where the unfolding intermediate is accumulated), and pH 2.0 (the acid-denaturing condition) were carried out by monitoring chromophore and tryptophan fluorescence. Kinetic on-pathway intermediates were accumulated during the folding on the refolding reaction from pH 2.0 to 7.5. However, the signal change corresponding to the conversion from the acid-denatured to the kinetic intermediate states was significantly reduced on the refolding reaction from pH 4.0 to pH 7.5, whereas only the signal change corresponding to the above conversion was observed on the refolding reaction from pH 2.0 to pH 4.0. These results indicate that the equilibrium unfolding intermediate is composed of an ensemble of the folding intermediate species accumulated during the folding reaction, and thus support a hierarchical model of protein folding. | |||||||||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 361, 号 5, p. 969-982, 発行日 2006-09-01 |
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| 出版者 | ||||||||||||
| 出版者 | Elsevier | |||||||||||
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| 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/10.1016/j.jmb.2006.07.009 | |||||||||||
| 関連名称 | 10.1016/j.jmb.2006.07.009 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2006 Elsevier Ltd. | |||||||||||
