| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1933602 | Biochemical and Biophysical Research Communications | 2009 | 4 Pages |
Abstract
Zic family proteins have five C2H2-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.
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Authors
Kumiko Sakai-Kato, Yoshinori Umezawa, Katsuhiko Mikoshiba, Jun Aruga, Naoko Utsunomiya-Tate,