Architectonics of a bacterial flagellin filament subunit

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Abstract
Flagellins of two Escherichia coli strains and their tryptic fragments were studied by different methods. Probabilities of secondary structure formation were also calculated for all flagellins with a known primary structure. The obtained data permit one to suggest a model for the flagellin molecule consisting of a central part responsible for antigenic properties and terminals responsible for polymerization. The central part is variable in length from a few amino acid residues to three‐four hundred depending on the bacterial species. The terminal parts consist of about 160 amino acid residues from the N‐end and 100 from the C‐end.