1. Grigor Arakelov, PhD
2. Osip Osipov
3. Harutyun Sahakyan

The Laboratory of computational modelling has been founded in 2007 on the basis of Laboratory of Organ specific Proteins. Main priority of the Laboratory is to use modern methods of bioinformatics and computational biology for modelling and in silico analysis of the processes of protein-protein, protein-ligand interactions and its regulation. For example, modelling of dynamic complex formation between glycolytic enzymes bring better understanding of enzyme-enzyme interaction and its functional consequences and gave a serious arguments in favour of metabollon formation and intermediate metabolite channelling. Investigation of tubulin-cytostatics interaction had serious implications in terms of practical use in the case of genetically determined FMF treatment. Recent research is focused on detailed in silico analysis of different domens and motives of pyrin-main protein, mutations of which are responsible for FMF manifestation- with apoptosis factors. It revealed new ways to control development of FMF.
In the research process capacity of own computer cluster, work station and internationally available supercomputers has been used.
The Laboratory plays lead role in running of the Department of Bioinformatics, Bioengineering and Molecular Biology at Slavonic University.

Currently the Laboratory of computation modelling of biological processes is implementing the project founded by National Academy of Sciences of the Republic of Armenia.

1. D. Hakobyan, K. Nazaryan, Molecular dynamics simulation of complex formation and possibility of channelling between Phosphoglycerate Mutase and Enolase. Biophys. J. 2131-Pos/B479, 2006.
2. D. Hakobyan, K. Nazaryan, “Study of Interactions between Neuron-Specific Enolase and B-type Phosphoglycerate Mutase with Molecular Dynamics Simulations”. Abstract Biophysical Journal for 54th Annual Meeting, 2009.
3. D. Hakobyan, K. Nazaryan, “Molecular Dynamics Study of Interaction and Substrate Channeling between Neuron-Specific Enolase and B-type Phosphoglycerate Mutase”. Proteins/Bioinformatics/ 2010, 78 (7), 1691-1704.
4. Hakobyan D., Varzhabetyan L., Nazaryan K. Molecular dynamics of α-tubulin and indibulin interaction. The New Armenian Medical Journal, 2010, 4 (1), 55-56.
5. L. R. Varzhabetyan, D. V. Glazachev, and K. B. Nazaryan. Molecular Dynamics Simulation Study of Tubulin Dimer Interaction with Cytostatics. Molecular Biology, 2012, Vol. 46, No. 2, pp. 316–321.