title: Determination of distance of intra-molecular hydrogen bonding in (Ala-Gly)15 with silk I form after removal of the effect of MAS frequency in REDOR experiment.
abstract: It is important to know the structure of silk I (Bombyx mori silk structure before spinning in the solid state) in order to understand the mechanism of fiber formation at the atomic level. In this study, 15N-dephased, 13C-observe REDOR has been carried out to determine the atomic distance of intra-molecular hydrogen bond between the 13C=O carbon of the 14th Gly residue and the 15N nitrogen of the 17th Ala residue of (AG)(6)A[1-13C]GAG[15N]AG(AG)(6) with silk I form after removal of the effect of MAS frequency on the re-coupling. The distance was determined to be 4.3A, which confirmed the intra-molecular hydrogen bonding formation between these two atomic sites.
authors.affiliation: Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
authors.forename: Tsunenori
authors.initials: T
authors.lastname: Kameda
authors.forename: Chenhua
authors.initials: C
authors.lastname: Zhao
authors.forename: Jun
authors.initials: J
authors.lastname: Ashida
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Asakura
mesh_terms: D000409:Alanine / Q000737:chemistry; D005998:Glycine / Q000737:chemistry; D006860:Hydrogen Bonding; D019476:Insect Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D047011:Silk
chemical_list: D019476:Insect Proteins; D010455:Peptides; D047011:Silk; D000409:Alanine; D005998:Glycine