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

作　　者：Shenlin Wang 

机构地区：[1]East China University of Science and Technology,Shanghai,200037,China

出　　处：《Magnetic Resonance Letters》2023年第1期85-86,I0004,共3页磁共振快报（英文）

基　　金：the National Natural Science Foundation of China(22274050,21874004,91953104);the Fundamental Research Funds for the Central Universities.

摘　　要：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(https://pubs.acs.org/doi/10.1021/jacs.2c10240).

关 键 词：INTERACTION NMR MERCURY 

分 类 号：O57[理学—粒子物理与原子核物理]