title: The serine-proline turn: a novel hydrogen-bonded template for designing peptidomimetics.
abstract: Serine-Proline (SP) dipeptide motifs have been shown to form unique hydrogen-bonding patterns in protein crystal structures. Peptides were designed to mimic these patterns by forming the 6 + 10 and the 9 + 10 hydrogen-bonded rings. Factors that contribute to the formation of SP turns include controlling backbone flexibility and amino acid chirality along with creating a hydrophobic environment around the intramolecular hydrogen bonds.
authors.affiliation: Center for Advanced Drug Research (CADRE), SRI International, 140 Research Drive, Harrisonburg, Virginia 22802, USA.
authors.forename: Benben
authors.initials: B
authors.lastname: Song
authors.forename: Martha G
authors.initials: MG
authors.lastname: Bomar
authors.forename: Patrick
authors.initials: P
authors.lastname: Kibler
authors.forename: Krishna
authors.initials: K
authors.lastname: Kodukula
authors.forename: Amit K
authors.initials: AK
authors.lastname: Galande
mesh_terms: D006860:Hydrogen Bonding; D008958:Models, Molecular; D008968:Molecular Conformation; D057786:Peptidomimetics / Q000737:chemistry*; D011392:Proline / Q000737:chemistry; D012694:Serine / Q000737:chemistry
chemical_list: D057786:Peptidomimetics; D012694:Serine; D011392:Proline