Thermal fluctuation is sufficient to explain allosteric changes in local protein dynamics

Summary

Thermal fluctuation is sufficient to explain (allosteric changes) in local protein dynamics (1). This is in contrast to a “domino model” of propagation of effects as proposed by (2).

Details

Per (3):

“proteins and other biological macromolecules may have evolved to take functional advantage not only of mean conformational states but also of the inevitable thermal fluctuations about the mean.”

See also

• Mutation of allosteric residues can influence the equilibrium dynamics of designed proteins

1.

Cooper A, Dryden DTF. Allostery without conformational change. European Biophysics Journal. 1984;11(2):103–9. Available from: https://doi.org/10.1007/bf00276625

2.

Monod J, Wyman J, Changeux J-P. On the nature of allosteric transitions: A plausible model. Journal of Molecular Biology. 1965;12(1):88–118. Available from: https://doi.org/10.1016/s0022-2836(65)80285-6

3.

Wankowicz SA, Fraser JS. Advances in uncovering the mechanisms of macromolecular conformational entropy. Nature Chemical Biology. 2025;21(5):623–34. Available from: https://doi.org/10.1038/s41589-025-01879-3