Magic angle spinning and oriented sample solid-state NMR structural restraints combine for influenza a M2 protein functional insights.

ABSTRACT: As a small tetrameric helical membrane protein, the M2 proton channel structure is highly sensitive to its environment. As a result, structural data from a lipid bilayer environment have proven to be essential for describing the conductance mechanism. While oriented sample solid-state NMR has provided a high-resolution backbone structure in lipid bilayers, quaternary packing of the helices and many of the side-chain conformations have been poorly restrained. Furthermore, the quaternary structural stability has remained a mystery. Here, the isotropic chemical shift data and interhelical cross peaks from magic angle spinning solid-state NMR of a liposomal preparation strongly support the quaternary structure of the transmembrane helical bundle as a dimer-of-dimers structure. The data also ex

SUBMITTER: Can TV 

PROVIDER: S-EPMC3415580 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature