Project : Computational Studies on Intrinsically Disordered Proteins Harbouring Disease causing Missense Mutations
The research mainly focuses on human protein-protein interaction networks (PPINs) and the role of conformational variability of intrinsically disordered proteins(IDPs) as hubs in rendering multiple interactions. A considerable part of this work will be devoted to explore the conformational space of IDPs by means of Molecular Dynamics and investigate how interaction promiscuity may arise as a result of multiple conformations possible for IDPs and how missense mutations may affect some of these conformations.
We have also been involved in the two collaborative works. First project was involved in the identification of isologous and heterologous interfaces of the RnaseE of E.coli and suggested some of the residues for site directed mutation, which were suspected to involved in dimer stabilization.
The second collaboration work was involved in the study of structural effects of missense mutations of GALNS that cause mucopolysaccharidosis IVA.
Conferences / Workshops Attended