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.
Research Institute of Pharmaceutical Sciences, Musashino University, 1-1-20 Shinmachi, Nishitokyo-shi, Tokyo, 202-8585, Japan.
Kumiko
K
Sakai-Kato
Yoshinori
Y
Umezawa
Katsuhiko
K
Mikoshiba
Jun
J
Aruga
Naoko
N
Utsunomiya-Tate
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