Possible three-dimensional models for the polypeptide backbone structure of alamethicin

Michael E. Johnson*, Tai Te Wu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Based on an empirical procedure of predicting polypeptide backbone structures of proteins, an attempt was made to construct possible three-dimensional models for the secondary structure of alamethicin. Two chemical properties were used to limit the number of possible models: the presence of seven to eight α-aminoisobutyric acid residues whose conformations were quite restricted, and a covalent bond between the proline residue at position 1 and the glutamic acid residue at position 17. The predicted structures appear very compact and show features in agreement with circular dichroism and optical rotatory dispersion results, nuclear magnetic resonance measurements, and compressed monolayer studies.

Original languageEnglish (US)
Pages (from-to)183-192,IN1-IN4,193-195
JournalJournal of Theoretical Biology
Issue number1
StatePublished - Jul 21 1976

ASJC Scopus subject areas

  • Statistics and Probability
  • Modeling and Simulation
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Agricultural and Biological Sciences(all)
  • Applied Mathematics


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