title: Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape.
abstract: The long-range side-chain repulsion between the (1R,2R,3R,5R)-2-amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.
authors.affiliation: Institute of Pharmaceutical Chemistry, University of Szeged, H-6720, Szeged, Hungary.
authors.forename: Anasztázia
authors.initials: A
authors.lastname: Hetényi
authors.forename: Zsolt
authors.initials: Z
authors.lastname: Szakonyi
authors.forename: István M
authors.initials: IM
authors.lastname: Mándity
authors.forename: Eva
authors.initials: E
authors.lastname: Szolnoki
authors.forename: Gábor K
authors.initials: GK
authors.lastname: Tóth
authors.forename: Tamás A
authors.initials: TA
authors.lastname: Martinek
authors.forename: Ferenc
authors.initials: F
authors.lastname: Fülöp
mesh_terms: D002264:Carboxylic Acids / Q000737:chemistry*; D003508:Cycloheptanes / Q000737:chemistry*; D004123:Dimethylamines / Q000737:chemistry*; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
chemical_list: D002264:Carboxylic Acids; D003508:Cycloheptanes; D004123:Dimethylamines; D009842:Oligopeptides