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

The use of the time-resolved X-ray solution scattering for studies of globular proteins

https://ir.soken.ac.jp/records/4306
https://ir.soken.ac.jp/records/4306
f0bd9bba-fe2b-4028-b587-1f730ad4f411
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-17
タイトル
タイトル The use of the time-resolved X-ray solution scattering for studies of globular proteins
タイトル
言語 en
タイトル The use of the time-resolved X-ray solution scattering for studies of globular proteins
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

WEKO 2361

KUWAJIMA, Kunihiro

Search repository
ARAI, Munehito

× ARAI, Munehito

WEKO 2491

ARAI, Munehito

Search repository
et, al.

× et, al.

WEKO 3119

et, al.

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
抄録
内容記述タイプ Abstract
内容記述 In order to improve the low signal-to-noise ratio of the time-resolved small-angle X-ray scattering, we have used a two-dimensional X-ray detector with a beryllium-windowed X-ray image intensifier and a charge-coupled device as an image sensor, and applied this to studies on (1) the kinetic folding reaction of α-lactalbumin, which accumulates the molten globule-like intermediate at an early stage of refolding and (2) the cooperative conformational transition of Escherichia coli chaperonin GroEL induced by ATP, which occurs in an allosteric manner between the close and open conformational states. In the α-lactalbumin reaction, we have firmly established the equivalence between the kinetic intermediate and the equilibrium molten globule state, and obtained further information about dehydration from the highly hydrated folding intermediate during a late stage of refolding. In the chaperonin study, we have successfully observed the kinetics of the allosteric transition of GroEL that occurs with a rate constant of about 3–4 s-1 at 5°C. The combination of the time-resolved X-ray scattering with other spectroscopic techniques such as circular dichroism and intrinsic fluorescence is thus very effective in understanding the conformational transitions of proteins and protein complexes.
書誌情報 Spectroscopy: An International Journal
en : Spectroscopy: An International Journal

巻 16, 号 3-4, p. 127-138, 発行日 2002
出版者
出版者 IOS Press
ISSN
収録物識別子タイプ ISSN
収録物識別子 0712-4813
権利
権利情報 ©2002 IOS Press
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