A model for ninefold symmetry in α keratin and cilia

P. Satir, B. Satir

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

The dimensions of the α helix are such that certain simple repeats of a small number of amino acids within a helical protein can generate ninefold symmetry. The chemical data for α keratin suggest that within this molecule total or partial repeats might occur every 22 or 44 amino acids, accounting for the pattern of nine seen in electron microscope images of α keratin microfibrils, if the postulated repeating sequence contains a binding site such that spatial extension is possible. Centrioles and their derivatives may be generated via further extension by a fundamentally similar morphogenetic process.

Original languageEnglish (US)
Pages (from-to)123-124,IN1,125-128
JournalJournal of Theoretical Biology
Volume7
Issue number1
StatePublished - Jul 1964

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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

Cite this

Satir, P., & Satir, B. (1964). A model for ninefold symmetry in α keratin and cilia. Journal of Theoretical Biology, 7(1), 123-124,IN1,125-128.