Dimerization of a flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
2014 (English)In: Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, Vol. 32, no 3, 406-415 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2014. Vol. 32, no 3, 406-415 p.
flocculent protein, oligomerization, homology modelling, binding free energy, protein-protein interactions
Biochemistry and Molecular Biology Biophysics
IdentifiersURN: urn:nbn:se:kth:diva-141285DOI: 10.1080/07391102.2013.770374ISI: 000329823600006ScopusID: 2-s2.0-84892637903OAI: oai:DiVA.org:kth-141285DiVA: diva2:696163
QC 201402132014-02-132014-02-132014-02-28Bibliographically approved