Albert Y. Lau

The paper develops a method using transfer entropy to analyze directional information flow in proteins, identifying key residues involved in allosteric communication and demonstrating its utility in capturing dynamic changes.

This study defines the substrate binding and activation mechanism of FtsW using simulations, mutagenesis, and assays, revealing conserved residues and structural constraints involved in lipid II binding and catalysis.

This study identifies ion permeation pathways in AMPARs using cryo-EM and MD simulations, showing how mutations affect ion flow and susceptibility to blockage.

This paper develops a computational method to study protein allostery, applying it to SARS-CoV-2 main protease to explore dihedral angles' role in allosteric signaling.