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Dimerization of a flocculent protein from Moringa oleifera: experimental evidence and in silico interpretation
KTH, School of Biotechnology (BIO), Industrial Biotechnology.
KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.
KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.ORCID iD: 0000-0003-0185-5724
KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.
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2014 (English)In: Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, E-ISSN 1538-0254, Vol. 32, no 3, 406-415 p.Article in journal (Refereed) Published
Abstract [en]

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.
Keyword [en]
flocculent protein, oligomerization, homology modelling, binding free energy, protein-protein interactions
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:kth:diva-141285DOI: 10.1080/07391102.2013.770374ISI: 000329823600006Scopus ID: 2-s2.0-84892637903OAI: oai:DiVA.org:kth-141285DiVA: diva2:696163
Note

QC 20140213

Available from: 2014-02-13 Created: 2014-02-13 Last updated: 2017-12-06Bibliographically approved

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Murugan, Natarajan ArulSrivastava, VaibhavÅgren, Hans

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