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Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase
https://ir.soken.ac.jp/records/4313
https://ir.soken.ac.jp/records/431393e66582-6ec8-48be-8432-8a8ba37aaf0a
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-19 | |||||
| タイトル | ||||||
| タイトル | Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase | |||||
| タイトル | ||||||
| タイトル | Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase | |||||
| 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 |
ARAI, Munehito
× ARAI, Munehito× 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 | The unfolded state of a protein is an ensemble of a large number of conformations ranging from fully extended to compact structures. To investigate the effects of the difference in the unfolded-state ensemble on protein folding, we have studied the structure, stability, and folding of “circular” dihydrofolate reductase (DHFR) from Escherichia coli in which the N and C-terminal regions are cross-linked by a disulfide bond, and compared the results with those of disulfide-reduced “linear” DHFR. Equilibrium studies by circular dichroism, difference absorption spectra, solution X-ray scattering, and size-exclusion chromatography show that whereas the native structures of both proteins are essentially the same, the unfolded state of circular DHFR adopts more compact conformations than the unfolded state of the linear form, even with the absence of secondary structure. Circular DHFR is more stable than linear DHFR, which may be due to the decrease in the conformational entropy of the unfolded state as a result of circularization. Kinetic refolding measurements by stopped-flow circular dichroism and fluorescence show that under the native conditions both proteins accumulate a burst-phase intermediate having the same structures and both fold by the same complex folding mechanism with the same folding rates. Thus, the effects of the difference in the unfolded state of circular and linear DHFRs on the refolding reaction are not observed after the formation of the intermediate. This suggests that for the proteins with close termini in the native structure, early compaction of a protein molecule to form a specific folding intermediate with the N and C-terminal regions in close proximity is a crucial event in folding. If there is an enhancement in the folding reflecting the reduction in the breadth of the unfolded-state ensemble for circular DHFR, this acceleration must occur in the sub-millisecond time-range. | |||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 329, 号 4, p. 779-791, 発行日 2003-06-13 |
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| 出版者 | ||||||
| 出版者 | Elsevier | |||||
| ISSN | ||||||
| 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/S0022-2836(03)00511-4 | |||||
| 関連名称 | 10.1016/S0022-2836(03)00511-4 | |||||
| 権利 | ||||||
| 権利情報 | © 2003 Elsevier Science Ltd. | |||||
