title: [Arrangement of molecular packing of collagen in fibrils].
abstract: This study analyses all possible models of molecular packing of collagen in quasi-hexagonal lattice. Models which contain microfibril compressed to place molecular axes on quasi-hexagonal lattice are refused since in this case molecules occupy non-equivalent positions. The present research has shown that there exist only four different kinds of lateral arrangement (plus their mirror images) with the molecules placed in equivalent positions and only two of them were considered previously as possible models of packing in quasi-hexagonal lattice. These two models are proved to be in obvious contradiction with intermolecular covalent crosslink data. One of the two models which remained is in complete accordance with crosslink data. This model is characterized by sheets of non-staggered molecules with neighbouring sheets being staggered axially by 66.8 nm (1 D).
mesh_terms: D000818:Animals; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D046911:Macromolecular Substances; D011487:Protein Conformation; D051381:Rats; D013623:Tail
chemical_list: D046911:Macromolecular Substances; D003094:Collagen
vernacular_title: Skhema molekuliarnoĭ upakovki kollagena v fibrillakh.