Stability and Folding Behavior Analysis of Zinc-Finger Using Simple ModelsReport as inadecuate




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1

College of Informatics, South China Agricultural University, Guangzhou 510642, China

2

Institute of Applied Mechanics and Biomedical Engineering, Taiyuan University of technology, Taiyuan 030024, China

3

College of Chemistry and Life Science, Leshan Teachers College, Leshan 614000, China





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Abstract 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. View Full-Text

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





Author: Shan Chang 1,* , Xiong Jiao 2, Jian-Ping Hu 3, Yan Chen 1 and Xu-Hong Tian 1,*

Source: http://mdpi.com/



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