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Helical and Expanded Conformation of Equine β-Lactoglobulin in the Cold-denatured State
https://ir.soken.ac.jp/records/4323
https://ir.soken.ac.jp/records/43238a41dbcb-44f6-40aa-b9fb-5c528bed2a09
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-20 | |||||
| タイトル | ||||||
| タイトル | Helical and Expanded Conformation of Equine β-Lactoglobulin in the Cold-denatured State | |||||
| タイトル | ||||||
| タイトル | Helical and Expanded Conformation of Equine β-Lactoglobulin in the Cold-denatured State | |||||
| 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 |
YAMADA, Yoshiteru
× YAMADA, Yoshiteru× 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 thermal unfolding transition of equine β-lactoglobulin (ELG) was investigated by circular dichroism (CD) over a temperature range of −15 °C to 85 °C. In the presence of 2 M urea, a cooperative unfolding transition was observed both with increasing and decreasing temperature. The CD spectrum indicated that the heat and cold-denatured states of ELG have substantial secondary structures but lack persistent tertiary packing of the side-chains. In order to clarify the relation between the heat or cold-denatured state and the acid-denatured (A) state characterized previously, we have attempted to observe the temperature dependence of the CD spectrum at pH 1.5. The CD spectrum in the heat-denatured state is similar to that in the A state. The CD spectrum in the A state does not change cooperatively with increasing temperature. These results indicate that the heat-denatured state and the A state are the same structural state. On the other hand, the CD intensity at acid pH cooperatively increased with decreasing temperature. The CD spectrum at low temperature and acid pH is consistent with that in the cold-denatured state. Therefore, the cold-denatured state is distinguished from the heat-denatured state or the A state, and ELG assumes a larger amount of non-native α-helices in the cold-denatured state. Small angle X-ray scattering and analytical ultracentrifugation have indicated that ELG assumes an expanded chain-like conformation in the cold-denatured state in contrast to the compact globular conformation in the A state. The relation between the molecular size and the helical content in the partially folded states is discussed. | |||||
| 書誌情報 |
Journal of Molecular Biology en : Journal of Molecular Biology 巻 350, 号 2, p. 338-348, 発行日 2005-07-08 |
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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/j.jmb.2005.05.003 | |||||
| 関連名称 | 10.1016/j.jmb.2005.05.003 | |||||
| 権利 | ||||||
| 権利情報 | © 2005 Elsevier Ltd. | |||||
