Multi-scale Approaches to Dynamical Transmission of Protein Allostery

Townsend, PD; Rodgers, TL; Pohl, E; Wilson, MR; Cann, MJ; McLeish, TCB

Abstract

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.

Citation

Townsend, P., Rodgers, T., Pohl, E., Wilson, M., Cann, M., & McLeish, T. (2015, January). Multi-scale Approaches to Dynamical Transmission of Protein Allostery. Presented at Physical Biology of Proteins and Peptides, Mexico City, Mexico

• Presentation Conference Type: Conference Paper (published)
• Conference Name: Physical Biology of Proteins and Peptides
• Start Date: Jan 31, 2015
• Publication Date: Oct 30, 2015
• Deposit Date: Nov 12, 2015
• Publisher: Springer Verlag
• Pages: 141-152
• Book Title: Physical Biology of Proteins and Peptides: Theory, Experiment, and Simulation
• ISBN: 9783319216867
• DOI: https://doi.org/10.1007/978-3-319-21687-4_8
• Public URL: https://durham-repository.worktribe.com/output/1123270