title: Neutron diffraction studies of collagen in fully mineralized bone.
abstract: Neutron diffraction measurements have been made of the equatorial and meridional spacings of collagen in fully mineralized mature bovine bone and demineralized bone collagen, in both wet and dry conditions. The collagen equatorial spacing in wet mineralized bovine bone is 1.24 nm, substantially lower than the 1.53 nm value observed in wet demineralized bovine bone collagen. Corresponding spacings for dry bone and demineralized bone collagen are 1.16 nm and 1.12 nm, respectively. The collagen meridional long spacing in mineralized bovine bone is 63.6 nm wet and 63.4 nm dry. These data indicate that collagen in fully mineralized bovine bone is considerably more closely packed than had been assumed previously, with a packing density similar to that of the relatively crystalline collagens such as wet rat tail tendon. The data also suggest that less space is available for mineral within the collagen fibrils in bovine bone than had previously been assumed, and that the major portion of the mineral in this bone must be located outside the fibrils.
mesh_terms: D000125:Achilles Tendon / Q000032:analysis; D000818:Animals; D001842:Bone and Bones / Q000032:analysis*; D002417:Cattle; D003094:Collagen / Q000032:analysis*; D008903:Minerals / Q000378:metabolism*; D009502:Neutrons; D012542:Scattering, Radiation; D014961:X-Ray Diffraction
chemical_list: D008903:Minerals; D003094:Collagen