title: Left-handed topology of super-secondary structure formed by aligned alpha-helix and beta-hairpin.
abstract: A novel super-secondary structure common for many non-homological proteins is considered. This folding pattern, consisting of adjacent along the chain alpha-helix and beta-hairpin, has an aligned packing. It is found that one of the two possible 'mirror-symmetrical' topologies is observed in proteins. The alpha-helix + beta-hairpin structures have a similar pattern of hydrophobic residues in their amino acid sequences. The remaining part of a molecule or a domain is almost always located on the same side of the considered folding pattern. These results can be used in the prediction of three-dimensional protein structure and protein design.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Moscow Region.
authors.forename: A V
authors.initials: AV
authors.lastname: Kajava
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment