Abstract
Allostery forms the basis of intra-molecular communications in various enzymes, however the underlying conformational changes are largely elusive. Recently, we have proposed to employ an elastic model based normal mode analysis to investigate the allosteric transitions in several molecular nanomachines (including myosin II, DNA polymerase and chaperonin GroEL). After combining with bioinformatics analysis of the evolutionary sequence variations, we have been able to identify the highly conserved and robust modes of collective motions that are capable of transmitting molecular signals over long distances.
Keywords: Allostery, chaperonin, elastic network model, myosin, normal mode analysis, polymerase
Current Protein & Peptide Science
Title: Allosteric Transitions in Biological Nanomachines are Described by Robust Normal Modes of Elastic Networks
Volume: 10 Issue: 2
Author(s): Wenjun Zheng, Bernard R. Brooks and D. Thirumalai
Affiliation:
Keywords: Allostery, chaperonin, elastic network model, myosin, normal mode analysis, polymerase
Abstract: Allostery forms the basis of intra-molecular communications in various enzymes, however the underlying conformational changes are largely elusive. Recently, we have proposed to employ an elastic model based normal mode analysis to investigate the allosteric transitions in several molecular nanomachines (including myosin II, DNA polymerase and chaperonin GroEL). After combining with bioinformatics analysis of the evolutionary sequence variations, we have been able to identify the highly conserved and robust modes of collective motions that are capable of transmitting molecular signals over long distances.
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Cite this article as:
Zheng Wenjun, Brooks R. Bernard and Thirumalai D., Allosteric Transitions in Biological Nanomachines are Described by Robust Normal Modes of Elastic Networks, Current Protein & Peptide Science 2009; 10 (2) . https://dx.doi.org/10.2174/138920309787847608
DOI https://dx.doi.org/10.2174/138920309787847608 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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