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Updated: Jun 23, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Stability of folding structure of Zic zinc finger proteins
Kumiko Sakai-Kato1, Yoshinori Umezawa, Katsuhiko Mikoshiba
1Research Institute of Pharmaceutical Sciences, Musashino University, 1-1-20 Shinmachi, Nishitokyo-shi, Tokyo, 202-8585, Japan.
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.
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