ログイン
言語:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

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

A folding model of α-lactalbumin deduced from the three-state denaturation mechanism

https://ir.soken.ac.jp/records/4117
https://ir.soken.ac.jp/records/4117
b2f3338e-0132-4b81-a6b2-953168735944
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-12-24
タイトル
タイトル A folding model of α-lactalbumin deduced from the three-state denaturation mechanism
タイトル
タイトル A folding model of α-lactalbumin deduced from the three-state denaturation mechanism
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 KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

KUWAJIMA, Kunihiro

Search repository
抄録
内容記述タイプ Abstract
内容記述 It has been shown that α-lactalbumin undergoes a three-state denaturation, involving a helical intermediate state, on treatment with guanidine hydrochloride. The unfolding of the protein and the characteristics of the intermediate state are examined by means of circular dichroism, difference spectra and pH-jump measurements to investigate the temperature dependence and kinetic properties of the unfolding and refolding, the pH dependence of the transition between the intermediate and the fully unfolded states, and the effect of disulphide bond reduction on the stabilization of the intermediate.

The results show that the long-range specific interactions such as specific electrostatic interactions and disulphide linkages are not important for stabilizing the intermediate, and that the transition between the intermediate and the fully unfolded states is extremely rapid (a relaxation time of less than one millisecond) and may correspond to the helix-coil transition of a polypeptide backbone. On the other hand, the activation parameters of the transition between the native and the intermediate states have suggested that the final stabilization by charge-pair interactions is preceded by hydrophobic interactions in the process of going from the intermediate to the native state.

The mechanism of folding of the protein is discussed, and the folding process from the fully unfolded to the native state is apparently divided into at least three main steps: (1) the formation of incipient helical structures dictated by local interactions; (2) the packing of the helical segments accompanied with hydrophobic interactions; (3) the final stabilization by the electrostatic interactions. The relevance to the current theoretical results on protein folding is also discussed.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 114, 号 2, p. 241-258, 発行日 1977-08-05
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/10.1016/0022-2836(77)90208-X
関連名称 10.1016/0022-2836(77)90208-X
権利
権利情報 © 1977 Published by Elsevier Ltd.
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:27:35.400959
Show All versions

Share

Mendeley Twitter Facebook Print Addthis

Cite as

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR 2.0
  • OAI-PMH JPCOAR 1.0
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX

Confirm


Powered by WEKO3


Powered by WEKO3