Mechanics of Allostery: Contrasting the Induced Fit and Population Shift Scenarios.

ABSTRACT: In allosteric proteins, binding a ligand can affect function at a distant location, for example, by changing the binding affinity of a substrate at the active site. The induced fit and population shift models, which differ by the assumed number of stable configurations, explain such cooperative binding from a thermodynamic viewpoint. Yet, understanding what mechanical principles constrain these models remains a challenge. Here, we provide an empirical study on 34 proteins supporting the idea that allosteric conformational change generally occurs along a soft elastic mode presenting extended regions of high shear. We argue, based on a detailed analysis of how the energy profile along such a mode depends on binding, that in the induced fit scenario, there is an optimal stiffness ka∗ ∼ 1/N fo

SUBMITTER: Ravasio R 

PROVIDER: S-EPMC7031744 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature