Structure refinement and diffuse streak scattering of silk (Bombyx mori).
Reexamination of the crystal structure of silk (Bombyx mori) was carried out by X-ray diffraction method. Four molecular chains are contained in the rectangular unit cell with parameters, a = 9.38 A, b = 9.49 A, and c (fiber axis) = 6.98 A, and the space group P2(1)-C(2)2. Silk assumes the statistical crystal structure, in which two antipolar-antiparallel sheet structures with different orientations statistically occupy a crystal site with the ratio 2:1. The molecular conformation is essentially the same pleated sheet structure as Marsh, Corey and Pauling proposed. However, the sheet structure formed by hydrogen bonds assumes the antipolar antiparallel structure different from that proposed by Marsh, Corey and Pauling, in which the methyl groups of alanine residues alternately point to both sides of the sheet structure along the hydrogen bonding direction. The crystalline region of silk is composed of stacking of two antipolar antiparallel sheet structures with different orientations.
Takahashi
Y
Y
Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Japan.
Gehoh
M
M
Yuzuriha
K
K
D000818:Animals; D012831:Bombyx / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019476:Insect Proteins / Q000737:chemistry*; D008958:Models, Molecular; D015233:Models, Statistical; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry; D047011:Silk
D019476:Insect Proteins; D047011:Silk; D012694:Serine