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

Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy

https://ir.soken.ac.jp/records/4281
https://ir.soken.ac.jp/records/4281
348808e5-9cea-48d6-9abb-daf066e5da74
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-11
タイトル
タイトル Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy
タイトル
タイトル Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy
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 MIZUGUCHI, Mineyuki

× MIZUGUCHI, Mineyuki

MIZUGUCHI, Mineyuki

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ARAI, Munehito

× ARAI, Munehito

ARAI, Munehito

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KE, Yue

× KE, Yue

KE, Yue

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NITTA, Katsutoshi

× NITTA, Katsutoshi

NITTA, Katsutoshi

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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 The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of α-lactalbumin, a homologous protein of equine lysozyme. The kinetic unfolding and refolding of the protein were induced by concentration jumps of the denaturant and measured by stopped-flow circular dichroism. The observed unfolding and refolding curves both agreed well with a single-exponential function. However, in the kinetic refolding reactions below 3 M guanidine hydrochloride, a burst-phase change in the circular dichroism was present, and the burst-phase intermediate in the kinetic refolding is shown to be identical with the molten globule state observed in the equilibrium unfolding. Under a strongly native condition, virtually all the molecules of equine lysozyme transform the structure from the unfolded state into the molten globule, and the subsequent refolding takes place from the molten globule state. The transition state of folding, which may exist between the molten globule and the native states, was characterized by investigating the guanidine hydrochloride concentration-dependence of the rate constants of refolding and unfolding. More than 80% of the hydrophobic surface of the protein is buried in the transition state, so that it is much closer to the native state than to the molten globule in which only 36% of the surface is buried in the interior of the molecule. It is concluded that all the present results are best explained by a sequential model of protein folding, in which the molten globule state is an obligatory folding intermediate on the pathway of folding.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 283, 号 1, p. 265-277, 発行日 1998-10-16
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 0022-2836
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1006/jmbi.1998.2100
関連名称 10.1006/jmbi.1998.2100
権利
権利情報 © 1998 Academic Press
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