Summary
Allostery can be mediated by changes in thermal fluctuations without a change in mean structure (1,2). This is one possible mechanism, in contrast to but not excluding a “domino model” of propagated structural changes as proposed by (3).
Details
Per (4):
“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
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.
Tzeng S-R, Kalodimos CG. Protein activity regulation by conformational entropy. Nature. 2012;488(7410):236–40. Available from: https://doi.org/10.1038/nature11271
3.
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
4.
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