PD Townsend
Multi-scale Approaches to Dynamical Transmission of Protein Allostery
Townsend, PD; Rodgers, TL; Pohl, E; Wilson, MR; Cann, MJ; McLeish, TCB
Authors
Contributors
Luis Olivares-Quiroz
Editor
Orlando Guzmán-López
Editor
Hector Eduardo Jardón-Valadez
Editor
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). Multi-scale Approaches to Dynamical Transmission of Protein Allostery. In L. Olivares-Quiroz, O. Guzmán-López, & H. E. Jardón-Valadez (Eds.), Physical Biology of Proteins and Peptides: Theory, Experiment, and Simulation (141-152). https://doi.org/10.1007/978-3-319-21687-4_8
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 |
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