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Architectonics of a bacterial flagellin filament subunit
Author(s) -
Fedorov O.V.,
Kostyukova A.S.,
Pyatibratov M.G.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81048-2
Subject(s) - flagellin , protein filament , protein subunit , escherichia coli , chemistry , amino acid , protein primary structure , polymerization , amino acid residue , protein secondary structure , biochemistry , peptide sequence , polymer , organic chemistry , gene
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.