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Cooperativity, connectivity, and folding pathways of multidomain proteins
http://hdl.handle.net/2237/20615
http://hdl.handle.net/2237/206156efeef9f-d9e0-47b7-b342-4eb366593e4a
名前 / ファイル | ライセンス | アクション |
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2014-10-30 | |||||
タイトル | ||||||
タイトル | Cooperativity, connectivity, and folding pathways of multidomain proteins | |||||
言語 | en | |||||
著者 |
Itoh, Kazuhito
× Itoh, Kazuhito× Sasai, Masaki |
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アクセス権 | ||||||
アクセス権 | open access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | energy landscape theory | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | structure-based model | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | circular permutation | |||||
抄録 | ||||||
内容記述 | Multidomain proteins are ubiquitous in both prokaryotic and eukaryotic proteomes. Study on protein folding, however, has concentrated more on the isolated single domains of proteins, and there have been relatively few systematic studies on the effects of domain–domain interactions on folding. We here discuss this issue by examining human γD-crystallin, spore coat protein S, and a tandem array of the R16 and R17 domains of spectrin as example proteins by using a structure-based model of folding. The calculated results consistently explain the experimental data on folding pathways and effects of mutational perturbations, supporting the view that the connectivity of two domains and the distribution of domain–domain interactions in the native conformation are factors to determine kinetic and equilibrium properties of cooperative folding. | |||||
言語 | en | |||||
内容記述タイプ | Abstract | |||||
出版者 | ||||||
言語 | en | |||||
出版者 | National Academy of Sciences | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプresource | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
出版タイプ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1073/pnas.0804512105 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 1091-6490 | |||||
書誌情報 |
en : Proceedings of the National Academy of Sciences of the United States of America 巻 105, 号 37, p. 13865-13870, 発行日 2008-09 |
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著者版フラグ | ||||||
値 | publisher | |||||
URI | ||||||
識別子 | http://dx.doi.org/10.1073/pnas.0804512105 | |||||
識別子タイプ | DOI | |||||
URI | ||||||
識別子 | http://hdl.handle.net/2237/20615 | |||||
識別子タイプ | HDL |