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

Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme by Stopped-Flow Circular Dichroism

https://ir.soken.ac.jp/records/4325
https://ir.soken.ac.jp/records/4325
d423e634-bf69-41ea-90a6-a48b4dbf415c
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-24
タイトル
タイトル Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme by Stopped-Flow Circular Dichroism
タイトル
タイトル Characterization of Kinetic Folding Intermediates of Recombinant Canine Milk Lysozyme 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 NAKAO, Masaharu

× NAKAO, Masaharu

NAKAO, Masaharu

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KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

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et, al.

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et, al.

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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 intermediate in the equilibrium unfolding of canine milk lysozyme induced by a denaturant is known to be very stable with characteristics of the molten globule state. Furthermore, there are at least two kinetic intermediates during refolding of this protein:  a burst-phase (first) intermediate formed within the dead time of stopped-flow measurements and a second intermediate that accumulates with a rate constant of 22 s-1. To clarify the relationships of these intermediates with the equilibrium intermediate, and also to characterize the structural changes of the protein during refolding, here we studied the kinetic refolding reactions using stopped-flow circular dichroism at 10 different wavelengths and obtained the circular dichroism spectra of the intermediates. Comparison of the circular dichroism spectra of the intermediates, as well as the absence of observed kinetics in the refolding from the fully unfolded state to the equilibrium intermediate, has demonstrated that the burst-phase intermediate is equivalent to the equilibrium intermediate. The difference circular dichroism spectrum that represented changes from the kinetic intermediate to the native state had characteristics of an exciton coupling band, indicating that specific packing of tryptophan residues in this protein occurred in this phase. From these findings, we propose a schematic model of the refolding of canine milk lysozyme that is consistent with the hierarchical mechanism of protein folding.
書誌情報 Biochemistry
en : Biochemistry

巻 44, 号 17, p. 6685-6692, 発行日 2005-04-07
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 0006-2960
DOI
識別子タイプ DOI
関連識別子 http://doi.org/10.1021/bi050082+
関連名称 10.1021/bi050082+
権利
権利情報 © 2005 American Chemical Society
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