Stability of folding structure of Zic zinc finger proteins.
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.
Sakai-Kato
Kumiko
K
Research Institute of Pharmaceutical Sciences, Musashino University, 1-1-20 Shinmachi, Nishitokyo-shi, Tokyo, 202-8585, Japan.
Umezawa
Yoshinori
Y
Mikoshiba
Katsuhiko
K
Aruga
Jun
J
Utsunomiya-Tate
Naoko
N
D000818:Animals; D002614:Chelating Agents / Q000737:chemistry; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D017510:Protein Folding; D055550:Protein Stability; D014157:Transcription Factors / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*; D016335:Zinc Fingers
D002614:Chelating Agents; D014157:Transcription Factors; D015032:Zinc