title: An improved capping unit for stabilizing the ends of associated β-strands.
abstract: Understanding protein beta structures has been hindered by the challenge of designing small, well-folded β-sheet systems. A β-capping motif was previously designed to help solve this problem, but not without limitations, as the termini of this β-cap were not fully available for chain extension. Combining Coulombic side chain attractions with a Trp/Trp edge-to-face interaction we produced a new capping motif that provided greater β-sheet stability. This stability was maintained even in systems lacking a turn locus with a high propensity for chain direction reversal. The Coulombic cap was shown to improve β-sheet stability in a number of difficult systems, hence providing an additional tool for protein structure and folding studies.
authors.affiliation: Department of Chemistry, University of Washington, Seattle, WA 98195, United States.
authors.forename: Jordan M
authors.initials: JM
authors.lastname: Anderson
authors.affiliation: Department of Chemistry, University of Washington, Seattle, WA 98195, United States.
authors.forename: Brandon L
authors.initials: BL
authors.lastname: Kier
authors.affiliation: Department of Chemistry, University of Washington, Seattle, WA 98195, United States.
authors.forename: Alexander A
authors.initials: AA
authors.lastname: Shcherbakov
authors.affiliation: Department of Chemistry, University of Washington, Seattle, WA 98195, United States.
authors.forename: Niels H
authors.initials: NH
authors.lastname: Andersen
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*
chemical_list: D004220:Disulfides; D010455:Peptides; D011506:Proteins
keywords: Beta Hairpin; Beta sheet; Capping stabilization; Peptide; Trp/Trp interaction