Literature DB >> 3981637

Neutron diffraction studies of collagen in fully mineralized bone.

L C Bonar, S Lees, H A Mook.   

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.

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Year:  1985        PMID: 3981637     DOI: 10.1016/0022-2836(85)90090-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  36 in total

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7.  Interpreting the equatorial diffraction pattern of collagenous tissues in the light of molecular motion.

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8.  Primary structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization.

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Review 9.  The Mineral-Collagen Interface in Bone.

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10.  Fine powdering exposes the mineral-protected collagen of bone to protease digestion.

Authors:  J J Wu; D R Eyre
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