title: Determining dihedral angles and local structure in silk peptide by 13C-2H REDOR.
abstract: 13C-2H REDOR NMR experiments were performed on 30-residue (AlaGly)15 silk I mimics of Bombyx mori silk fibroin to gain structural details about the elusive structure of the silk I conformation. 13C,2H-labeling strategies are illustrated for measuring individual dihedral angles in peptides and for determining local structure by REDOR. A major turn of type II character is found in the region Gly(14)-Ala(17).
authors.affiliation: Department of Chemistry, West Virginia University, Morgantown, WV 26506, USA. terry.gullion@mail.wvu.edu
authors.forename: Terry
authors.initials: T
authors.lastname: Gullion
authors.forename: Raghuvansh
authors.initials: R
authors.lastname: Kishore
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Asakura
mesh_terms: D000818:Animals; D012831:Bombyx / Q000737:chemistry; D002247:Carbon Isotopes; D003903:Deuterium; D005349:Fibroins / Q000737:chemistry*; D019476:Insect Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017433:Protein Structure, Secondary; D047011:Silk
chemical_list: D002247:Carbon Isotopes; D019476:Insect Proteins; D047011:Silk; D005349:Fibroins; D003903:Deuterium