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

Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme

https://ir.soken.ac.jp/records/4293
https://ir.soken.ac.jp/records/4293
c627d6e1-ec1d-4065-ace5-78fdf13dda94
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-13
タイトル
タイトル Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme
タイトル
タイトル Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme
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 KOSHIBA, Takumi

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KOSHIBA, Takumi

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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 Here, we show that an unfolded intermediate of canine milk lysozyme is extraordinarily stable compared with that of the other members of the lysozyme-α-lactalbumin superfamily, which has been studied previously. The stability of the intermediate of this protein was investigated using calorimetry, CD spectroscopy, and NMR spectroscopy, and the results were interpreted in terms of the structure revealed by X-ray crystallography at a resolution of 1.85 Å to an R-factor of 17.8%. On the basis of the results of the thermal unfolding, this protein unfolds in two clear cooperative stages, and the melting temperature from the intermediate to the unfolded states is about 20 °C higher than that of equine milk lysozyme. Furthermore, the 1H NMR spectra of canine milk lysozyme at 60 °C, essentially 100% of which exists in the intermediate, showed that small resonance peaks that arise from ring-current shifts of aliphatic protons are still present in the upfield region from 0 to −1 ppm. The protein at this temperature (60 °C) and pH 4.5 has been found to bind 1-anilino-naphthalene-8-sulfonate (ANS) with enhancement of the fluorescence intensity compared with that of native and thermally unfolded states. We interpret that the extraordinarily stable intermediate is a molten globule state, and the extraordinary stabilization of the molten globule state comes from stronger protection around the C- and D-helix of the aromatic cluster region due to the His-21 residue. The conclusion helps to explain how the molten globule state acquires its structure and stability.
書誌情報 Biochemistry
en : Biochemistry

巻 39, 号 12, p. 3248-3257, 発行日 2000
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/bi991525a
関連名称 10.1021/bi991525a
権利
権利情報 © 2000 American Chemical Society
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