Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.

@article{Tang2009StructureAM,
  title={Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy.},
  author={Ming Yue Tang and Mei Hong},
  journal={Molecular bioSystems},
  year={2009},
  volume={5 4},
  pages={317-22}
}
The membrane-bound structure, lipid interaction, and dynamics of the arginine-rich beta-hairpin antimicrobial peptide PG-1 as studied by solid-state NMR are highlighted here. A variety of solid-state NMR techniques, including paramagnetic relaxation enhancement, (1)H and (19)F spin diffusion, dipolar recoupling distance experiments, and 2D anisotropic-isotropic correlation experiments, are used to elucidate the structural basis for the membrane disruptive activity of this representative beta… CONTINUE READING

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