title: The folding and design of repeat proteins: reaching a consensus.
abstract: Although they are widely distributed across kingdoms and are involved in a myriad of essential processes, until recently, repeat proteins have received little attention in comparison to globular proteins. As the name indicates, repeat proteins contain strings of tandem repeats of a basic structural element. In this respect, their construction is quite different from that of globular proteins, in which sequentially distant elements coalesce to form the protein. The different families of repeat proteins use their diverse scaffolds to present highly specific binding surfaces through which protein-protein interactions are mediated. Recent studies seek to understand the stability, folding and design of this important class of proteins.
authors.affiliation: Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
authors.forename: Ewan R G
authors.initials: ER
authors.lastname: Main
authors.forename: Sophie E
authors.initials: SE
authors.lastname: Jackson
authors.forename: Lynne
authors.initials: L
authors.lastname: Regan
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017089:Ankyrin Repeat; D009154:Mutation; D015202:Protein Engineering; D017510:Protein Folding