Alamethicin. A rich model for channel behavior.

@article{Hall1984AlamethicinAR,
  title={Alamethicin. A rich model for channel behavior.},
  author={James Edwin Hall and Igor Vodyanoy and T M Balasubramanian and Garland R. Marshall},
  journal={Biophysical journal},
  year={1984},
  volume={45 1},
  pages={233-47}
}
Alamethicin, a 20-amino acid peptide, has been studied for a number of years as a model for voltage-gated channels. Recently both the x-ray structure of alamethicin in crystal and an NMR solution structure have been published (Fox and Richards, 1982. Bannerjee et al., 1983). Both structures show that the amino end of the molecule forms a stable alpha-helix nine or 10 residues in length and that the COOH-terminal ends exhibits a variable hydrogen bonding pattern. We have used synthetic analogues… CONTINUE READING

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