Structural And Dynamics Characterization Of Membrane Proteins Using Static Solid State Nuclear Magnetic Resonance Spectroscopy

Solid-state nuclear magnetic resonance (NMR) provides a unique approach for structure determination and functional studies of membrane proteins in a native lipid bilayer environment. Here, polarization inversion spin exchange at magic angle (PISEMA) experiments of aligned samples were applied to study the proton channel, M2 protein transmembrane portion (M2-TMD) from influenza A virus and other intact full length membrane proteins. The challenges of membrane protein structure characterization utilizing static aligned sample, including sample preparation, sample stability induced by RF heating, PISEMA experiment set up were discussed.