Multi-scale approaches to dynamical transmission of protein allostery

Philip D. Townsend*, Thomas L. Rodgers, Ehmke Pohl, Mark R. Wilson, Martin J. Cann, Tom C.B. McLeish

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapter


We review the idea that allosteric interactions can be transmitted not by structural switching but by the more subtle route of modulation of the amplitude of thermally-activated global dynamical modes in allosteric proteins. The effect is naturally addressed and explored through coarse-grained models of protein dynamics, but can be linked to atomistic models of substrate binding at the fine scale, and to themodynamic free energies at the macroscopic scale. A remarkable specificity at the residue level emerges: allosteric proteins possess a set of ‘control sites’ whose modification by single-point mutation may alter allosteric free-energies non-perturbatively.

Original languageEnglish
Title of host publicationPhysical Biology of Proteins and Peptides
Subtitle of host publicationTheory, Experiment, and Simulation
Number of pages12
ISBN (Electronic)9783319216874
ISBN (Print)9783319216867
Publication statusPublished - 23 Oct 2015


  • CAP protein
  • Conformational changes
  • Elastic network models
  • Molecular simulation
  • Multiscale modelling
  • Normal modes

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