We investigate the solution structure of human eNOS protein by using synchrotron small-angle X-ray scattering (SAXS). The pair-correlation analysis of the profile shows the radius of gyration (R-g) and maxima dimension (D-max) of 6.87 +/- 0.03 nm and 22 nm, respectively. The ratio of D-max and R-g revealed that the protein was an extended conformation. The ab initio shape determination and rigid-body calculations were performed to reconstruct the real-space structure of eNOS in solution. The result shows that human eNOS form homodimer form in solution with the closed contact of two oxygenase domains.
Date:
2012-04
Relation:
Chinese Journal of Physics. 2012 Apr;50(2):344-348.
