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Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme
https://ir.soken.ac.jp/records/4293
https://ir.soken.ac.jp/records/4293c627d6e1-ec1d-4065-ace5-78fdf13dda94
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-13 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme | |||||||||||
| タイトル | ||||||||||||
| タイトル | Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme | |||||||||||
| 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 |
KOSHIBA, Takumi
× KOSHIBA, Takumi
× 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 | Here, we show that an unfolded intermediate of canine milk lysozyme is extraordinarily stable compared with that of the other members of the lysozyme-α-lactalbumin superfamily, which has been studied previously. The stability of the intermediate of this protein was investigated using calorimetry, CD spectroscopy, and NMR spectroscopy, and the results were interpreted in terms of the structure revealed by X-ray crystallography at a resolution of 1.85 Å to an R-factor of 17.8%. On the basis of the results of the thermal unfolding, this protein unfolds in two clear cooperative stages, and the melting temperature from the intermediate to the unfolded states is about 20 °C higher than that of equine milk lysozyme. Furthermore, the 1H NMR spectra of canine milk lysozyme at 60 °C, essentially 100% of which exists in the intermediate, showed that small resonance peaks that arise from ring-current shifts of aliphatic protons are still present in the upfield region from 0 to −1 ppm. The protein at this temperature (60 °C) and pH 4.5 has been found to bind 1-anilino-naphthalene-8-sulfonate (ANS) with enhancement of the fluorescence intensity compared with that of native and thermally unfolded states. We interpret that the extraordinarily stable intermediate is a molten globule state, and the extraordinary stabilization of the molten globule state comes from stronger protection around the C- and D-helix of the aromatic cluster region due to the His-21 residue. The conclusion helps to explain how the molten globule state acquires its structure and stability. | |||||||||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 39, 号 12, p. 3248-3257, 発行日 2000 |
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| 出版者 | ||||||||||||
| 出版者 | American Chemical Society | |||||||||||
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| 収録物識別子タイプ | ISSN | |||||||||||
| 収録物識別子 | 0006-2960 | |||||||||||
| DOI | ||||||||||||
| 識別子タイプ | DOI | |||||||||||
| 関連識別子 | http://doi.org/10.1021/bi991525a | |||||||||||
| 関連名称 | 10.1021/bi991525a | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2000 American Chemical Society | |||||||||||
