| Literature DB >> 19422807 |
Kumiko Sakai-Kato1, Yoshinori Umezawa, Katsuhiko Mikoshiba, Jun Aruga, Naoko Utsunomiya-Tate.
Abstract
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.Entities:
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Year: 2009 PMID： 19422807 DOI： 10.1016/j.bbrc.2009.04.151
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575