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  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

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/4155
42555362-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

KALNIN, Nikolay N

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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著者別名 桑島, 邦博

× 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
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.
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