Proton-Coupled Ion and Substrate Transport Across Biological Membrane
The extension of the hybrid-solvent CpHMD for transmembrane proteins has opened a door for obtaining previously unattainable insights into biological proton/ion transport. To pave the way, we demonstrated that CpHMD can directly reveal the atomic details of the pH-dependent conformational transitions of a proton channel, an antiporter, and a multi-drug efflux pump.
Zooming in on a small multidrug transporter reveals details of asymmetric protonation.
Yue Z, Chen W, Zgurskaya, H, and Shen J*,
Constant pH molecular dynamics reveals how proton release drives the conformational transition of a transmembrane efflux pump.
Chen W, Huang YD, and Shen J*,
Conformational activation of a transmembrane proton channel from constant pH molecular dynamics.
Huang YD, Chen W, Dotson DL, Beckstein O, and Shen J*,
Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA.