Modulation mechanism of aquaporins by mercury revealed by solid-state NMR and molecular dynamics simulations

In a recent paper,the structural basis of mercury-mediated changes in aquaporins'(AQPs)function has been revealed at the atomic level by solid-state nuclear magnetic resonance(ssNMR)spectroscopy and molecular dynamics(MD)simulations[1].This work has demonstrated an interesting case of metal ion-protein interaction.It provided valuable insights on how mercury ions achieve opposite regulations of AQP permeability by disrupting the hydrogen bonding network around arginine residues().