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Stability of folding structure of Zic zinc finger proteins |
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| Authors: | Kumiko Sakai-Kato Yoshinori Umezawa Jun Aruga Naoko Utsunomiya-Tate |
| Institution: | a Research Institute of Pharmaceutical Sciences, Musashino University, 1-1-20 Shinmachi, Nishitokyo-shi, Tokyo, 202-8585, Japan b National Institute of Health Sciences, Tokyo 158-8501, Japan c Laboratory for Developmental Neurobiology, RIKEN Brain Science Institute, Saitama 351-0198, Japan d Laboratory for Behavioral and Developmental Disorders, RIKEN Brain Science Institute, Wako-shi, Saitama 351-0198, Japan |
| 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. |
| Keywords: | ZF zinc finger NMR nuclear magnetic resonance CD circular dichroism PCR polymerase chain reaction LB Luria-Bertani DTT dithiothreitol DSC differential scanning calorimetry |
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