Statistical conformation of human plasma fibronectin

Fibronectin is a multifunctional glycoprotein (molecular mass, M = 530 kg/mol) of the extra cellular matrix (ECM) having a major role in cell adhesion. In physiological conditions, the conformation of this protein still remains debated and controversial. Here, we present a set of results obtained by scattering experiments. In 'native' conditions, the radius of gyration (R(g) = 15.3 ± 0.3 nm) was determined by static light scattering as well as small-angle neutron scattering. The hydrodynamic radius (R(H) = 11.5 ± 0.1 nm) was deduced from quasi-elastic light scattering measurements. These results imply a low internal concentration (M/R³(g/H)) compared to that of usual globular proteins. This is also confirmed by the ratio R(H)/R(g) = 0.75 ± 0.02 consistent with a Gaussian chain, whereas R(H)/R(g) = 1.3 for spherical shaped molecules. However, adding a denaturing agent (urea 8 M) increases R(g) by a factor 2. This means that fibronectin 'native' chain is not either completely unfolded. The average shape of fibronectin conformation was also probed by small-angle neutron scattering performed for reverse scattering vector q^-1 smaller than R(g) (0.2 < q^-1 < 15 nm). The measured form factor is in complete agreement with the form factor of a random string of 56 beads of 5 nm diameter. It rules out the possibility of unfolded chain as well as globular structures. These results have structural and biological implications as far as ECM organization is concerned.