Allosteric transitions in biological nanomachines are described by robust normal modes of elastic networks

Curr Protein Pept Sci. 2009 Apr;10(2):128-32. doi: 10.2174/138920309787847608.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Chaperonin 60 / chemistry*
  • DNA-Directed DNA Polymerase / chemistry*
  • Elasticity
  • Models, Molecular*
  • Myosin Type II / chemistry*
  • Nanostructures
  • Protein Conformation

Substances

  • Chaperonin 60
  • DNA-Directed DNA Polymerase
  • Myosin Type II