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Allosteric regulation

Proceedings of the National Academy of Sciences

Significance In allosteric proteins, binding a ligand affects activity at a distant site. The physical principles allowing for such an action at a distance are not well understood. Here we introduce a numerical scheme to evolve allosteric materials in which the number of solutions, their spatial architectures, and the correlations among them can be computed. We show that allostery in these materials uses recently discovered elastic edge modes near the active site to transmit information, and that correlations generated during evolution alone can reveal key aspects of this architecture.

Architecture and coevolution of allosteric materials