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Effect of an Alternative Disulfide Bond on the Structure, Stability, and Folding of Human Lysozyme
https://ir.soken.ac.jp/records/4300
https://ir.soken.ac.jp/records/4300fbe98ba3-5672-4c4f-a806-ff112d4524e5
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2014-03-14 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Effect of an Alternative Disulfide Bond on the Structure, Stability, and Folding of Human Lysozyme | |||||||||||
| タイトル | ||||||||||||
| タイトル | Effect of an Alternative Disulfide Bond on the Structure, Stability, and Folding of Human 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 |
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 | Human lysozyme has four disulfide bonds, one of which, Cys65−Cys81, is included in a long loop of the β-domain. A cysteine-scanning mutagenesis in which the position of Cys65 was shifted within a continuous segment from positions 61 to 67, with fixed Cys81, has previously shown that only the mutant W64CC65A, which has a nonnative Cys64−Cys81 disulfide, can be correctly folded and secreted by yeast. Here, using the W64CC65A mutant, we investigated the effects of an alternative disulfide bond on the structure, stability, and folding of human lysozyme using circular dichroism (CD) and fluorescence spectroscopy combined with a stopped-flow technique. Although the mutant is expected to have a different main-chain structure from that of the wild-type protein around the loop region, far- and near-UV CD spectra show that the native state of the mutant has tightly packed side chains and secondary structure similar to that of the wild-type. Guanidine hydrochloride-induced equilibrium unfolding transition of the mutant is reversible, showing high stability and cooperativity of folding. In the kinetic folding reaction, both proteins accumulate a similar burst-phase intermediate having pronounced secondary structure within the dead time of the measurement and fold into the native structure by means of a similar folding mechanism. Both the kinetic refolding and unfolding reactions of the mutant protein are faster than those of the wild-type, but the increase in the unfolding rate is larger than that of the refolding rate. The Gibbs' free-energy diagrams obtained from the kinetic analysis suggest that the structure around the loop region in the β-domain of human lysozyme is formed after the transition state of folding, and thus, the effect of the alternative disulfide bond on the structure, stability, and folding of human lysozyme appears mainly in the native state. | |||||||||||
| 書誌情報 |
Biochemistry en : Biochemistry 巻 39, 号 12, p. 3472-3479, 発行日 2000 |
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| 出版者 | ||||||||||||
| 出版者 | American Chemical Society | |||||||||||
| ISSN | ||||||||||||
| 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/10.1016/S0065-3233(00)53005-8 | |||||||||||
| 関連名称 | 10.1016/S0065-3233(00)53005-8 | |||||||||||
| 権利 | ||||||||||||
| 権利情報 | © 2000 American Chemical Society | |||||||||||
