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Envelope Structure of Human eNOS Protein Revealed by Small-Angle X-ray Scattering
並列摘要
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(subscript g)) and maxima dimension (D(subscript max)) of 6.87 ± 0.03 nm and 22 nm, respectively. The ratio of D(subscript max) and R(subscript 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.
並列關鍵字
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