Light-sensitive allosteric switch module, a broadly applicable protein engineering method, is used for the regulation of protein activity with tight temporal control and spatial precision.

Deep mutational scanning of a synthetic allosteric chimera revealed that a sparse set of mutations on the protein surface improved regulation.

Key allosteric residues are predicted based on sequence coevolution analysis, which serves as guidelines for allosteric drug design and optimization.

By measuring how multiple conformations shift in response to temperature, a new allosteric binding site is discovered for the phosphatase PTP1B.

The signaling ligand (p)ppGpp regulates the enzyme HPRT across species by binding to a novel class of conserved motif, yet its specificity is allosterically altered through evolution of enzyme oligomerization.

Specific residues within an enzyme integrate allosteric inputs that originate from distinct ligand-binding pockets.

A combination of equilibrium and nonequilibrium molecular dynamics simulations is an effective tool to study allosteric communications in ultrafast enzymes that show little or no conformational changes.

A catalytically dead paralog activates its cognate enzyme through an allosteric mechanism that combined structural and phylogenomic analysis indicates arose through acquisition of a dimerization domain, suggesting a general model for how complex allostery evolves.

Integrating co-evolution with long-range dynamic coupling analysis allows to identify allosteric mutations that modulate binding affinity, and this approach can be used to design lectins with enhanced binding affinity.

Mechanistic studies of glutamine synthetase reveals how the complex quaternary structure organizations of a supramolecular enzyme provides a platform necessary for intricate activity regulation machinery to take place.