Cross-linkage sites in type I collagen fibrils studied by neutron diffraction.
Cross-links in tendon collagen are essential for the biomechanical strength of healthy tissue. The nature and position of these cross-links has long been a subject for conjecture. We have approached this problem in a non-destructive manner, by studying neutron diffraction from collagen fibrils that have been specifically deuterated by reduction at keto-amine and Schiff base groups with sodium borodeuteride (NaB2H4). The intensities of the first 23 meridional reflections were recorded for both native and reduced tendons. These data were used to calculate the neutron-scattering density profile of the 67 nm (D) repeat of type I collagen fibrils in rat tail tendon. This approach not only succeeds in determining the location of the cross-linkage sites with respect to the fibril structure, as projected onto the fibre axis, but also presents a novel form of the isomorphous derivative solution to the phase problem.
Wess
T J
TJ
Department of Biochemistry, University of Edinburgh Medical School, Scotland.
Miller
A
A
Bradshaw
J P
JP
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003094:Collagen; D009502:Neutrons; D051381:Rats; D011919:Rats, Inbred Strains; D013710:Tendons; D014961:X-Ray Diffraction
D003094:Collagen