Determining dihedral angles and local structure in silk peptide by 13C-2H REDOR.
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).
Gullion
Terry
T
Department of Chemistry, West Virginia University, Morgantown, WV 26506, USA. terry.gullion@mail.wvu.edu
Kishore
Raghuvansh
R
Asakura
Tetsuo
T
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
D002247:Carbon Isotopes; D019476:Insect Proteins; D047011:Silk; D005349:Fibroins; D003903:Deuterium