Dimerization of a flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
2014
Pavankumar, A. | Kayathri, R. | Murugan, N. | Zhang, Q. | Srivastava, V. | Okoli, C. | Bulone, V. | Rajarao, G. | Ågren, H.
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.
Afficher plus [+] Moins [-]Asalapuram R. Pavankumar, Rajarathinam Kayathri, Natarajan A. Murugan, Qiong Zhang, Vaibhav Srivastava, Chuka Okoli, Vincent Bulone, Gunaratna K. Rajarao and Hans Ågren
Afficher plus [+] Moins [-]Mots clés AGROVOC
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