Molecular Dynamics and Conformational Flexibility in Heat Shock Protein 60.2 of Mycobacterium Tuberculosis

HSP 60.2 plays important role in pathogenesis of Mycobacterium tuberculosis causing tuberculosis. This chaperonin comprises of three domains namely-apical, intermediate and equatorial which assists in proper protein folding thus preventing aggregation of unfolded polypeptides. To evaluate the structural changes during protein folding, conformations of HSP 60.2 were monitored during 10 ns time scale. Molecular dynamic simulations are used to study the large amount of molecular and biomolecular conformations with the use of high end computational assistance. The Principal component analysis and clustering techniques are used for revealing major conformational changes that occur in the MD simulation. Normal mode analysis was also performed to study the conformation and direction of motion of a protein under study for a large time scale simulation. These studies suggest that functional behavior of protein that depends on the structure. Chaperonin 60.2 is not only plays a role as protein folding machinery, but also an immunologically important biomolecule. Hence it is provided and drawn a clear path between role of chaperon in protein folding and their role in the infection showing the immunological importance of Heat Shock Protein 60.2.