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.
Bibliographical noteFunding Information:
ARP acknowledges European Commission’s Erasmus Mundus External Cooperation Window (EURINDIA) and the support of Mrs. Alphonsa Lourdudoss, Coordinator at the Royal Institute of Technology (KTH), towards his postdoctoral scholarship.
- binding free energy
- Flocculent protein
- homology modelling
- protein-protein interactions