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Selected Mutations in a Mesophilic Cytochrome c Confer the Stability of a Thermophilic Counterpart

https://hiroshima.repo.nii.ac.jp/records/2007230
https://hiroshima.repo.nii.ac.jp/records/2007230
e80c2f6d-283a-44f8-91d4-415bb9d7f915
名前 / ファイル ライセンス アクション
J. J. Biol. Chem_275_37824.pdf (283.8 KB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Selected Mutations in a Mesophilic Cytochrome c Confer the Stability of a Thermophilic Counterpart
言語 en
作成者 Hasegawa, Jun

× Hasegawa, Jun

en Hasegawa, Jun

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Uchiyama, Susumu

× Uchiyama, Susumu

en Uchiyama, Susumu

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Tanimoto, Yuko

× Tanimoto, Yuko

en Tanimoto, Yuko

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Mizutani, Masayuki

× Mizutani, Masayuki

en Mizutani, Masayuki

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Kobayashi, Yuji

× Kobayashi, Yuji

en Kobayashi, Yuji

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Sambongi, Yoshihiro

× Sambongi, Yoshihiro

en Sambongi, Yoshihiro

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Igarashi, Yasuo

× Igarashi, Yasuo

en Igarashi, Yasuo

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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
権利情報
権利情報 This research was originally published in the Journal of Biological Chemistry. Jun Hasegawa, Susumu Uchiyama, Yuko Tanimoto, Masayuki Mizutani, Yuji Kobayashi, Yoshihiro Sambongi and Yasuo Igarashi. Selected Mutations in a Mesophilic Cytochrome c Confer the Stability of a Thermophilic Counterpart. J. Biol. Chem. 2000; 275(48):37824-37828. © the American Society for Biochemistry and Molecular Biology.
内容記述
内容記述 Mesophilic cytochrome c551 of Pseudomonas aeruginosa (PA c551) became as stable as its thermophilic counterpart, Hydrogenobacter thermophilus cytochrome c552 (HT c552), through only five amino acid substitutions. The five residues, distributed in three spatially separated regions, were selected and mutated with reference to the corresponding residues in HT c552 through careful structure comparison. Thermodynamic analysis indicated that the stability of the quintuple mutant of PA c551 could be partly attained through an enthalpic factor. The solution structure of the mutant showed that, as in HT c552, there were tighter side chain packings in the mutated regions. Furthermore, the mutant had an increased total accessible surface area, resulting in great negative hydration free energy. Our results provide a novel example of protein stabilization in that limited amino acid substitutions can confer the overall stability of a natural highly thermophilic protein upon a mesophilic molecule.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported by a grant from the Japanese Ministry of Education, Science and Culture.
出版者
出版者 The American Society for Biochemistry and Molecular Biology, Inc.
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1074/jbc.M005861200
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M005861200
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9258
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1083-351X
開始ページ
開始ページ 37824
書誌情報 Journal of Biological Chemistry
Journal of Biological Chemistry

巻 275, 号 48, p. 37824-37828, 発行日 2000-12-01
旧ID 48608
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