Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition.

@article{Andreas2010MagicAS,
  title={Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition.},
  author={Loren B Andreas and Matthew T Eddy and Rafal M Pielak and James J. Chou and Robert G Griffin},
  journal={Journal of the American Chemical Society},
  year={2010},
  volume={132 32},
  pages={10958-60}
}
The tetrameric M2 proton channel from influenza A virus conducts protons at low pH and is inhibited by aminoadamantyl drugs such as amantadine and rimantadine (Rmt). We report magic angle spinning NMR spectra of POPC and DPhPC membrane-embedded M2(18-60), both apo and in the presence of Rmt. Similar line widths in the spectra of apo and bound M2 indicate that Rmt does not have a significant impact on the dynamics or conformational heterogeneity of this construct. Substantial chemical shift… CONTINUE READING

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