2009年7月
Stability of folding structure of Zic zinc finger proteins
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 384
- 号
- 3
- 開始ページ
- 362
- 終了ページ
- 365
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2009.04.151
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Zic family Proteins have five C(2)H(2)-type zinc finger (ZF) motifs. We physicochemically characterized the folding properties of Zic ZFs. Alteration of chelation with zinc ions and of hydrophobic interactions changed circular dichroism spectra, suggesting that they caused structural changes. The motifs were heat stable, but electrostatic interactions had little effect on structural stability. These results highlight the importance of chelating interactions and hydrophobic interactions for the stability of the folding structure of Zic ZF proteins. (C) 2009 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2009.04.151
- ISSN : 0006-291X
- Web of Science ID : WOS:000266647400017