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

Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra

https://ir.soken.ac.jp/records/4145
https://ir.soken.ac.jp/records/4145
235a5a19-cd98-4aae-b5a8-07e32aa648d4
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-01-15
タイトル
タイトル Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra
タイトル
タイトル Folding of staphylococcal nuclease-a studied by equilibrium and kinetic circular-dichroism spectra
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 SUGAWARA, Tatsuro

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SUGAWARA, Tatsuro

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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SUGAI, Shintaro

× SUGAI, Shintaro

SUGAI, Shintaro

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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 The urea-induced unfolding of staphylococcal nuclease A has been studied by circular dichroism both at equilibrium and by the kinetics of unfolding and refolding (pH 7.0 and 4.5 °C), as a function of Ca2+ and thymidine 3′,5′-diphosphate (pdTp) concentration. The results are as follows. (1) The unfolding transition is shifted to higher concentrations of urea by Ca2+ and pdTp, and the presence of both ligands further stabilizes the protein. (2) In the first stage of kinetic refolding, the peptide ellipticity changes rapidly within the dead time of stopped-flow measurement (15 ms), indicating accumulation of a transient intermediate. This intermediate is remarkably less stable than those of other globular proteins previously studied. (3) Dependence of the folding and unfolding rate constants on urea concentration indicates that the critical activated state of folding ("transition state") has considerable structural organization. The transition state does not, however, have the capacity to bind Ca2+ and pdTp, as indicated by the effects of these ligands on the unfolding rate constant. (4) There are at least four different phases in the refolding kinetics in native conditions below 1 M urea. In the absence of pdTp, there are two phases in unfolding, while in the presence of pdTp the unfolding kinetics show a single phase. Some characteristics of the transient intermediate and of the transition state for folding are discussed.
書誌情報 Biochemistry
en : Biochemistry

巻 30, 号 10, p. 2698-2706, 発行日 1991-03
出版者
出版者 American Chemical Society
ISSN
収録物識別子タイプ ISSN
収録物識別子 00062960
PubMed番号
識別子タイプ PMID
関連識別子 2001357
DOI
識別子タイプ DOI
関連識別子 http://doi.org/10.1021/bi00224a018
関連名称 10.1021/bi00224a018
権利
権利情報 © 1991 American Chemical Society
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