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Solution structure of human plasma fibronectin using small-angle X-ray and neutron scattering at physiological pH and ionic strength

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
255
Issue
2
Identifiers
DOI: 10.1016/0003-9861(87)90402-4
Keywords
  • Protein Structure And Function
Disciplines
  • Biology

Abstract

Abstract Human plasma fibronectin has been investigated at physiological pH and ionic strength, by using small-angle X-ray and neutron scattering techniques. The results indicate that the molecule is disc shaped with an axial ratio of about 1:10. In fact, an ellipsoid of revolution with semiaxes a = 1.44 nm and b = c = 13.8 nm is in agreement with the experimental scattering data, and can also fully explain the rather extreme hydrodynamic parameters reported for fibronectin. The X-ray data gave a radius of gyration of 8.9 nm and a molecular weight of 510,000, whereas the neutron data gave slightly larger values, 9.5 nm and 530,000, respectively. From the volume of the best fitting ellipsoid we obtain a degree of hydration of 0.61 g H 2O/g protein (dry weight). Neutron data, recorded at different D 2O concentrations in the solvent, gave a match point of 43% D 2O, which indicates that approximately 80% of the hydrogens bound to oxygen and nitrogen are exchangeable.

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