title: Novel sequences propel familiar folds.
abstract: Recent structure determinations have made new additions to a set of strikingly different sequences that give rise to the same topology. Proteins with a beta propeller fold are characterized by extreme sequence diversity despite the similarity in their three-dimensional structures. Several fold predictions, based in part on sequence repeats thought to match modular beta sheets, have been proved correct.
authors.affiliation: Department of Biochemistry, University of Cambridge, Tennis Court Road, CB2 1QW, Cambridge, United Kingdom.
authors.forename: Zahra
authors.initials: Z
authors.lastname: Jawad
authors.forename: Massimo
authors.initials: M
authors.lastname: Paoli
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D016415:Sequence Alignment
chemical_list: D011506:Proteins