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1.
Muscle Nerve ; 5(3): 238-46, 1982 Mar.
Article in English | MEDLINE | ID: mdl-7088022

ABSTRACT

The structure of striated muscle (thick and thin filaments, filament lattice, and collagen), peripheral nerve myelin, and tendon collagen were studied in tissues from dystrophic and normal mice using small-angle x-ray diffraction. There were increases in the amount of disorganized tissue in the dystrophic mice, and the time course of the changes was monitored over the first 42 weeks of life. As the dystrophic mice became older, the contractile apparatus of the muscles appeared to atrophy, while the amount of collagen increased. In general, the molecular structure and packing appeared to remain unchanged as the disease progressed, although changes in the relative amounts and the organization of proteins were noted. In both normal and dystrophic mice, the collagen periodicity (65.7 nm) was 2% smaller when detected in muscle tissue compared with that detected in tendon tissue.


Subject(s)
Muscles/pathology , Muscular Dystrophy, Animal/pathology , Peripheral Nerves/pathology , X-Ray Diffraction , Animals , Collagen/analysis , Mice , Muscles/physiopathology , Muscular Dystrophy, Animal/physiopathology , Myelin Sheath/analysis , Myelin Sheath/physiology , Peripheral Nerves/physiopathology , Tendons/pathology , Tendons/physiopathology
2.
Biophys J ; 26(2): 209-21, 1979 May.
Article in English | MEDLINE | ID: mdl-262416

ABSTRACT

An experimental procedure is developed to phase the reflections obtained in x-ray diffraction investigations of collagen in native wet tendons. Phosphotungstic acid was used for isomorphous addition in phase determination and was located by electron microscopy. Structure factors (with phases) were obtained from the electron microscopy data for the heavy metal. Structure-factor magnitudes for collagen with and without the heavy metal were obtained from the x-ray diffraction data. The first 10 orders were investigated. Standard Argand diagrams provided two solutions for each of these, except the weak sixth order. In each case, one of the two possible solutions agrees well with the phases proposed on theoretical grounds by Hulmes et al. The present results suggest that their other proposed phases are probably correct. An electron density profile along the unit cell of the fibril is presented that shows a distinct step, as expected on the basis of the hole-overlap model. The overlap region is 48% of the length of the unit cell.


Subject(s)
Collagen , Animals , Ducks , Mathematics , Microscopy, Electron , Protein Conformation , Tendons/analysis , X-Ray Diffraction
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