The automatic detection of known β-propeller structural motifs from protein tertiary structure

Structural-symmetry-related sequence patterns of the proteins of beta-propeller family

“…We think our classification scheme may be a balance of the propensities of both beta-preference and hydrophobicity because five of the stronger beta-formers are also hydrophobic. Furthermore, in most cases, a secondary structure prediction will be difficult to suggest the presence of repeat beta units because structural variations associated with the b-propeller architecture, corresponding to the number of bstrands in the blade, number of amino acid residues in equivalent b-strands in the different blades, the occurrence and locations of b-helices [24,25].…”