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Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model
American Journal of Bioscience and Bioengineering
Volume 3, Issue 6, December 2015, Pages: 162-168
Received: Dec. 16, 2015; Published: Dec. 17, 2015
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Authors
Lu Jin, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Nan Xiao, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Chunhua Li, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Jianjun Tan, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Xiaoyi Zhang, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China
Jiguo Su, College of Science, Yanshan University, Qinhuangdao, China
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Abstract
Glutamine-Binding Protein (GlnBP) from Escherichia coli is an extremely important periplasmic binding protein. Binding of glutamine at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. Because this process has a close relationship with protein function, studying this process has an important biological significance. It is very difficult for the existing experimental methods to obtain the conformational transition of GlnBP. In this paper, we studied the allosteric mechanism of GlnBP by using the adaptive Anisotropic Network Model (aANM) proposed by Bahar and obtained a relatively reasonable allosteric pathway. This work is helpful for the understanding the role of the topology structure in GlnBP conformational transition.
Keywords
Glutamine-Binding Protein, Adaptive Anisotropic Network Model, Allosteric Mechanism
To cite this article
Lu Jin, Nan Xiao, Chunhua Li, Jianjun Tan, Xiaoyi Zhang, Jiguo Su, Allosteric Transitions of Glutamine-Binding Protein Studied by the Elastic Network Model, American Journal of Bioscience and Bioengineering. Vol. 3, No. 6, 2015, pp. 162-168. doi: 10.11648/j.bio.20150306.14
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