title: Determination of intermolecular distance for a model peptide of Bombyx mori silk fibroin, GAGAG, with rotational echo double resonance.
abstract: Rotational echo double resonance NMR spectroscopy is applied for the determination of the distance of intermolecular chains of pentapeptide, GAGAG (G: Gly, A: Ala), a model typical of the crystalline domain in Bombyx mori silk fibroin. 1:4 mixture of G[1-(13)C]AGAG and GAG[(15)N]AG with antiparallel beta-sheet structure was used to determine the distance of intermolecular hydrogen bonding between adjacent molecules within pleated sheet and the (13)C-(15)N interatomic distance was determined to be 4.3 A. On the other hand, 1:4 mixture of GAG[1-(13)C]AG and GAG[(15)N]AG gave information on the interpleated sheet arrangement. When we assumed the same distances between two interpleated sheets, the distance was calculated to be 5.3 A and the angle (15)N-(13)C-(15)N was 180 degrees.
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: Yasumoto
authors.initials: Y
authors.lastname: Nakazawa
authors.forename: Junko
authors.initials: J
authors.lastname: Kazuhara
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Yamane
authors.forename: Tetsuo
authors.initials: T
authors.lastname: Asakura
mesh_terms: D000818:Animals; D012831:Bombyx; D005349:Fibroins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy
chemical_list: D005349:Fibroins