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Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism
https://ir.soken.ac.jp/records/4155
https://ir.soken.ac.jp/records/415542555362-a5e1-49f9-b7d1-5701e777a602
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| 公開日 | 2014-01-17 | |||||||||
| タイトル | ||||||||||
| タイトル | Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism | |||||||||
| タイトル | ||||||||||
| タイトル | Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism | |||||||||
| 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 |
KALNIN, Nikolay N
× KALNIN, Nikolay N
× 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 | Kinetics of refolding and unfolding of staphylococcal nuclease and its six mutants, each carrying single or double amino acid substitutions, are studied by stopped-flow circular dichroism measurements. A transient kinetic intermediate formed within 10 ms after refolding starts possesses a substantial part of the N-domain core β-structure, whereas helices are formed at the later stages. The structure of the kinetic intermediate is less organized than the structure that is known to be formed by a nuclease 1-136 fragment. Only the refolding kinetics are affected by the mutations in all the mutants except two in which the mutations have changed the native structure. From this result and also from the locations of the mutation sites, the major N-terminal domain of the nuclease in the transition state of folding has a structure nearly identical to the native one. On the other hand, the minor C-terminal domain has previously been shown to be still disorganized in the transition state. The effects of the amino acid substitutions on the stability of the native and the transition states are in good agreement with the changes in the hydration free energy, expected for the corresponding amino acid replacements in the unfolded polypeptide. Since side chains of all the mutated residues are not accessible to solvent in the native structure, the result suggests that it is the unfolded state that is mainly affected by the mutations. | |||||||||
| 書誌情報 |
Proteins: Structure, Function, and Bioinformatics en : Proteins: Structure, Function, and Bioinformatics 巻 23, 号 2, p. 163-176, 発行日 1995-10 |
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| 出版者 | ||||||||||
| 出版者 | Wiley-Blackwell | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 08873585 | |||||||||
| PubMed番号 | ||||||||||
| 識別子タイプ | PMID | |||||||||
| 関連識別子 | 8592698 | |||||||||
| DOI | ||||||||||
| 識別子タイプ | DOI | |||||||||
| 関連識別子 | https://doi.org/10.1002/prot.340230206 | |||||||||
| 関連名称 | 10.1002/prot.340230206 | |||||||||
| 権利 | ||||||||||
| 権利情報 | © 1995 Wiley-Liss, Inc. | |||||||||
