title: Model systems for beta-hairpins and beta-sheets.
abstract: beta-Sheets and alpha-helices are the two principal secondary structures in proteins. However, our understanding of beta-sheet structure lags behind that of alpha-helices, largely because, until recently, there was no model system to study the beta-sheet secondary structure in isolation. With the development of well-folded beta-hairpins, this is changing rapidly. Recent advances include: increased understanding of the relative contributions of turn, strand and sidechain interactions to beta-hairpin and beta-sheet stability, with the role of aromatic residues as a common subtheme; experimental and theoretical kinetic and thermodynamic studies of beta-hairpin and beta-sheet folding; de novo protein design, including all-beta structures, mixed alpha/beta motifs and switchable systems; and the creation of functional beta-hairpins.
authors.affiliation: Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.
authors.forename: Robert M
authors.initials: RM
authors.lastname: Hughes
authors.forename: Marcey L
authors.initials: ML
authors.lastname: Waters
mesh_terms: D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins