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

Journal Article · Mon Jun 01 04:00:00 EDT 1987 · Arch. Biochem. Biophys.; (United States)

DOI:https://doi.org/10.1016/0003-9861(87)90402-4· OSTI ID:6477400

Sjoeberg, B P; Pap, S; Osterlund, E; Osterlund, K; Vuento, M; Kjems, J

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/sub 2/O/g protein (dry weight). Neutron data, recorded at different D/sub 2/O concentrations in the solvent, gave a match point of 43% D/sub 2/O, which indicates that approximately 80% of the hydrogens bound to oxygen and nitrogen are exchangeable.

• Research Organization: Univ. of Goeteborg, Sweden
• OSTI ID: 6477400
• Journal Information: Arch. Biochem. Biophys.; (United States), Journal Name: Arch. Biochem. Biophys.; (United States) Vol. 2; ISSN ABBIA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AQUEOUS SOLUTIONS
COHERENT SCATTERING
DEUTERIUM
DIFFRACTION
DISPERSIONS
HYDROGEN ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MIXTURES
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
NUCLEI
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
PROTEINS
SCATTERING
SOLUTIONS
STABLE ISOTOPES
TRACER TECHNIQUES
X-RAY DIFFRACTION