A model for ninefold symmetry in α keratin and cilia

P. Satir, Birgit H. Satir

Research output: Contribution to journalArticle

10 Citations (Scopus)

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)
JournalJournal of Theoretical Biology
Volume7
Issue number1
StatePublished - Jul 1964
Externally publishedYes

Fingerprint

Keratin
Cilia
keratin
cilia
Keratins
Amino Acids
Amino acids
Centrioles
Microfibrils
Symmetry
centrioles
amino acids
electron microscopes
Binding sites
Helix
Microscope
binding sites
Electron microscopes
chemical derivatives
Binding Sites

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

A model for ninefold symmetry in α keratin and cilia. / Satir, P.; Satir, Birgit H.

In: Journal of Theoretical Biology, Vol. 7, No. 1, 07.1964.

Research output: Contribution to journalArticle

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