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

Asalapuram R. Pavankumar, Rajarathinam Kayathri, Natarajan A. Murugan, Qiong Zhang, Vaibhav Srivastava, Chuka Okoli, Vincent Bulone, Gunaratna K. Rajarao, Hans Ågren

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)406-415
Number of pages10
JournalJournal of Biomolecular Structure and Dynamics
Issue number3
Publication statusPublished - Mar 2014
Externally publishedYes

Bibliographical note

Funding 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
  • oligomerization
  • protein-protein interactions


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