Stability and Folding Behavior Analysis of Zinc-Finger Using Simple Models

International Journal of Molecular Sciences

Shan Chang²  Xiong Jiao³  Jian-Ping Hu¹  Yan Chen² 

[1] College of Chemistry and Life Science, Leshan Teacher’s College, Leshan 614000, China; E-Mail:;College of Informatics, South China Agricultural University, Guangzhou 510642, China; E-Mail:;Institute of Applied Mechanics and Biomedical Engineering, Taiyuan University of technology, Taiyuan 030024, China; E-Mail:

关键词: zinc finger;    folding pathway;    Gaussian network model;    anisotropy elastic network model;    Sp1f2;    FSD-1;   

DOI  :  10.3390/ijms11104014

来源: mdpi

【 摘 要 】

Zinc-fingers play crucial roles in regulating gene expression and mediating protein-protein interactions. In this article, two different proteins (Sp1f2 and FSD-1) are investigated using the Gaussian network model and anisotropy elastic network model. By using these simple coarse-grained methods, we analyze the structural stabilization and establish the unfolding pathway of the two different proteins, in good agreement with related experimental and molecular dynamics simulation data. From the analysis, it is also found that the folding process of the zinc-finger motif is predominated by several factors. Both the zinc ion and C-terminal loop affect the folding pathway of the zinc-finger motif. Knowledge about the stability and folding behavior of zinc-fingers may help in understanding the folding mechanisms of the zinc-finger motif and in designing new zinc-fingers. Meanwhile, these simple coarse-grained analyses can be used as a general and quick method for mechanistic studies of metalloproteins.

【 授权许可】

CC BY   
© 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.