Dimerization of a flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation

Abstract

Many proteins exist in dimeric and other oligomeric forms to gain stability and functional advantages. In this study, the dimerization property of a coagulant protein (MO₂.₁) from Moringa oleifera seeds was addressed through laboratory experiments, protein-protein docking studies and binding free energy calculations. The structure of MO₂.₁ was predicted by homology modelling, while binding free energy and residues-distance profile analyses provided insight into the energetics and structural factors for dimer formation. Since the coagulation activities of the monomeric and dimeric forms of MO₂.₁ were comparable, it was concluded that oligomerization does not affect the biological activity of the protein.