Dimerization of flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
(English)Article in journal (Refereed) Epub ahead of print
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.
IdentifiersURN: urn:nbn:se:kth:diva-94179PubMedID: 23662981OAI: oai:DiVA.org:kth-94179DiVA: diva2:525708
QP 20132012-05-092012-05-092013-05-31Bibliographically approved