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 language | English (US) |
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Pages (from-to) | 123-124,IN1,125-128 |
Journal | Journal of Theoretical Biology |
Volume | 7 |
Issue number | 1 |
DOIs | |
State | Published - Jul 1964 |
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