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The molten globule state of alpha-lactalbumin
https://ir.soken.ac.jp/records/4271
https://ir.soken.ac.jp/records/42716f1461cc-6763-4943-b8ad-c58c7630f368
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
1021.full (1.9 MB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2014-03-10 | |||||||
| タイトル | ||||||||
| タイトル | The molten globule state of alpha-lactalbumin | |||||||
| タイトル | ||||||||
| タイトル | The molten globule state of alpha-lactalbumin | |||||||
| 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 | |||||||
| 著者 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro
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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 molten globule state of alpha-lactalbumin is the best-characterized folding intermediate of globular proteins and has been studied intensively by various spectroscopic and physiochemical techniques, including stopped-flow CD and fluorescence spectroscopies, a hydrogen-exchange technique, 1H-NMR spectroscopy, disulfide-exchange chemistry, site-directed mutagenesis, and calorimetric techniques. This review summarizes recent studies. Major findings about the structure of the molten globule state are: 1) It is highly heterogeneous, having a highly structured alpha-helical domain with the beta-sheet domain being significantly unfolded; and 2) it is not a nonspecific, collapsed polypeptide but already has a native-like tertiary fold. These structural characteristics are essential to fully understand the thermodynamic properties of the molten globule state which are described in connection with a recently proposed computational approach to predict the structure of the molten globule state of a protein. Mutant proteins in which the stability of the molten globule state was changed were constructed. Studies of the equilibrium unfolding and kinetic refolding of the mutant proteins will provide further insight into the molten globule state as a folding intermediate. In spite of an initial expectation that the structure recognized by an Escherichia coli chaperone, GroEL, is the molten globule, the interaction of GroEL with alpha-lactalbumin in the molten globule state is much weaker than the interaction with more unfolded states of alpha-lactalbumin, a disulfide-reduced form, and disulfide rearranged species. | |||||||
| 書誌情報 |
FASEB Journal en : FASEB Journal 巻 10, 号 1, p. 102-109, 発行日 1996-01 |
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| 出版者 | ||||||||
| 出版者 | The Federation of American Society of Experimental Biology | |||||||
| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0892-6638 | |||||||
| DOI | ||||||||
| 関連タイプ | isIdenticalTo | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | https://doi.org/10.1096/fasebj.10.1.8566530 | |||||||
| 関連名称 | 10.1096/fasebj.10.1.8566530 | |||||||
| 権利 | ||||||||
| 権利情報 | © 1996 by The Federation of American Societies for Experimental Biology | |||||||
| 関連サイト | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | http://www.fasebj.org/site/misc/edpolicies.xhtml#Copyright_and_Permissions_Policy | |||||||
| 関連名称 | Copyright | |||||||
| フォーマット | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | application/pdf | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | VoR | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||
