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Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism
https://ir.soken.ac.jp/records/4119
https://ir.soken.ac.jp/records/4119eeb84a7e-c673-4db9-8a06-299eb15eebd3
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2013-12-24 | |||||
| タイトル | ||||||
| タイトル | Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism | |||||
| タイトル | ||||||
| タイトル | Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism | |||||
| 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 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro× SUGAI, Shintaro |
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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 thermal unfolding of α-lactalbumin has been studied by equilibrium measurements of aromatic difference spectra, and by kinetic measurements of the Joule heating temperature-jump. The unfolding at neutral pH is a reversible two-state transition. The equilibrium transition curves are analyzed by the nonlinear least squares method, which gives correct values of thermodynamic parameters based on the data in a wide range of temperature. The results are discussed in relation to the previous studies on the unfolding by guanidine hydrochloride or by acid. The thermally unfolded state, a partially unfolded species, is shown to be thermodynamically similar to but not identical with the acid state. The folding pathway deduced from the kinetic results is essentially consistent with the folding model of α-lactalbumin proposed previously. Large decreases in entropy and in heat capacity during the reversed activation suggest the packing of the folded segments by hydrophobic interactions, while the forward activation shows a marked temperature dependence, probably caused by the disruption of specific long-range interactions. | |||||
| 書誌情報 |
Biophysical Chemistry en : Biophysical Chemistry 巻 8, 号 3, p. 247-254, 発行日 1978-07 |
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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 | 0301-4622 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1016/0301-4622(78)87006-9 | |||||
| 関連名称 | 10.1016/0301-4622(78)87006-9 | |||||
| 権利 | ||||||
| 権利情報 | © 1978 Published by Elsevier B.V. | |||||
