Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMR.

@article{Yao2013MembranedependentCD,
  title={Membrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMR.},
  author={Hongwei Yao and Mei Hong},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 3},
  pages={563-76}
}
The entry of enveloped viruses into cells requires protein-catalyzed fusion of the viral and cell membranes. The structure-function relation of a hydrophobic fusion peptide (FP) in viral fusion proteins is still poorly understood. We report magic-angle-spinning solid-state NMR results of the membrane-bound conformation, dynamics, and lipid interactions of the FP of the F protein of the paramyxovirus, parainfluenza virus 5 (PIV5). (13)C chemical shifts indicate that the PIV5 FP structure depends… CONTINUE READING
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