title: Molecular bending and networks in a basement membrane-like collagen: packing in dogfish egg capsule collagen.
abstract: Low-angle X-ray diffraction data have been obtained from three mutually perpendicular axes through sheets of the collagenous egg capsule of the dogfish Scyliorhinus caniculus, a collagen that resembles type IV collagen. The data are interpreted in the light of the body of knowledge of the structure derived from transmission electron microscopy by Knight and Hunt. A model to account for the X-ray data is proposed incorporating the main dimensions of the Knight and Hunt model which are confirmed by the diffraction data. Several features of the diffraction patterns are not explained by the existing model however, and a new model is proposed to account for these features. This consists of antiparallel packed pairs of two mutually parallel molecules, each kinked and rotated so as to produce a four-fold helix resembling a crankshaft. This has the advantage of conferring intermolecular linkage in three dimensions throughout the structure with tetragonal symmetry and unit dimensions a = b = 22.6 nm, c (fibre axis direction) = 39.3 nm. The result is a fairly rigid open polygonal network or sponge-like architecture that is capable of accommodating large quantities of water and other molecules.
authors: H. H. Wills Physics Laboratory, University of Bristol, UK.
authors: L J
authors: LJ
authors: Gathercole
authors: E D
authors: ED
authors: Atkins
authors: E G
authors: EG
authors: Goldbeck-Wood
authors: K
authors: K
authors: Barnard
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000737:chemistry; D003094:Collagen / Q000737:chemistry*; D004284:Dogfish / Q000378:metabolism*; D005260:Female; D046911:Macromolecular Substances; D008958:Models, Molecular; D010063:Ovum / Q000737:chemistry; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D046911:Macromolecular Substances; D003094:Collagen