Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.

@article{Kovacs1999ValidationOT,
  title={Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.},
  author={F A Kovacs and Jack R Quine and Timothy A. Cross},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 14},
  pages={7910-5}
}
The monovalent cation selective channel formed by a dimer of the polypeptide gramicidin A has a single-stranded, right-handed helical motif with 6.5 residues per turn forming a 4-A diameter pore. The structure has been refined to high resolution against 120 orientational constraints obtained from samples in a liquid-crystalline phase lipid bilayer. These structural constraints from solid-state NMR reflect the orientation of spin interaction tensors with respect to a unique molecular axis… CONTINUE READING