Ruibin Liang

This study develops and benchmarks a multiscale free-energy method to predict light-responsive binding of ionizable photoswitchable inhibitors to eDHFR, showing that explicit treatment of protonation states is critical for accurate predictions.

This study develops a surfactant-guided strategy to improve protein-MOF integration by modulating interfacial design, showing increased encapsulation efficiency and MOF growth rate.

This study investigates the allosteric effects of the coupling cation in the melibiose transporter MelB by integrating structural, HDX-MS, and simulation data to reveal how cation binding enhances sugar-binding affinity through conformational restraint.

This study maps the atomic-level free energy landscape of Na+-coupled melibiose transport in MelBSt, revealing cooperative binding mechanisms and allosteric coupling between substrates.

This study identifies the distinct roles of key residues in the cation-binding pocket of MelBSt through structural analysis, free energy simulations, and biochemical experiments.

This study determines the structure and dynamics of a Na+-coupled sugar transporter, revealing how mobile barriers regulate substrate binding and release.