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Analysis of protein conformational transitions using elastic network model

  • SUNY Buffalo

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

5 Scopus citations

Abstract

In this chapter, we demonstrate the usage of a coarse-grained elastic network model to analyze protein conformational transitions in the NS3 helicase (NS3hel) of Hepatitis C virus (HCV). This analysis allows us to identify and visualize collective domain motions involved in the conformational transitions and predict the order of structural events during the transitions. It is highly efficient and applicable to many multi-domain protein structures which undergo large conformational changes to fulfill their functions. This method is made available through a Web server (http://enm.lobos.nih.gov).

Original languageEnglish
Title of host publicationProtein Dynamics
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Pages159-172
Number of pages14
ISBN (Print)9781627036573
DOIs
StatePublished - 2014

Publication series

NameMethods in Molecular Biology
Volume1084
ISSN (Print)1064-3745

Keywords

  • Coarse-grained model
  • Conformational transition
  • Elastic network model
  • Helicase
  • Normal mode analysis
  • Reaction coordinate
  • Transition pathway

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