Next Article in Journal
Characteristics of Lignin from Flax Shives as Affected by Extraction Conditions
Next Article in Special Issue
Characterization of a Deswapped Triple Mutant Bovine Odorant Binding Protein
Previous Article in Journal
Cyclin D1 Expression and the Inhibitory Effect of Celecoxib on Ovarian Tumor Growth in Vivo
Previous Article in Special Issue
Folding Mechanism of Beta-Hairpin Trpzip2: Heterogeneity, Transition State and Folding Pathways
Article Menu

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2010, 11(10), 4014-4034; doi:10.3390/ijms11104014

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

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 Teacher's College, Leshan 614000, China
*
Authors to whom correspondence should be addressed.
Received: 7 September 2010 / Revised: 1 October 2010 / Accepted: 9 October 2010 / Published: 19 October 2010
(This article belongs to the Special Issue Protein Folding 2011)
View Full-Text   |   Download PDF [805 KB, uploaded 19 June 2014]   |  

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.
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
Figures

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Chang, S.; Jiao, X.; Hu, J.-P.; Chen, Y.; Tian, X.-H. Stability and Folding Behavior Analysis of Zinc-Finger Using Simple Models. Int. J. Mol. Sci. 2010, 11, 4014-4034.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top