Liquid-liquid phase separation (LLPS) has received a gigantic attention and has emerged as the key regulatory mechanism for cellular compartmentalization in absence of membranes. Till now, we have unravelled the complicated interaction picture that dictates the diffusivity in homotypic protein condensates. In the coming years, we aim to elucidate the complex trade-off between protein-protein and protein-RNA interactions in heterotypic condensates of RNA binding proteins and how systematic post-translational modifications alter the balance between the two kind of interactions detailed above. Such trade-offs may dictate the reversal of disease like solid aggregates-to normal liquid-like condensates. 

Massively different sequences in intrinsically disordered proteins  astonishingly have tremendouly similar functionality!  We are yet to elucidate the entire molecular grammar of how diverse sequence mediated  IDP conformational ensembles converge toward same functionality.  In addition, a fundamental question of interest that bothers us,  can disorder act as mode of cellular communication?

Water at biomolecular interfaces have the potential to mediate the thermodynamics of biomolecular assemblies. Hydration waters not only play a crucial role in determining stability of the biomolecules rather the properties of hydration water must reflect the properties of the heterogeneous surface and may spatially vary along protein surface itself.  We aim to probe the heterogenity of equlibrium water dynamics  at heterogenous protein surfaces which may have a signalling efficiency for molecular recognition.h

Toward a complete description of cytoplasm? Can multi-component polydispersed liquids be a simpler description of cytoplasmic complexities? 

Collective excitations in dipolar liquids or binary mixtures and their contribution toward solvation dynamics is well-known in literature now. Even such sub-THz frequency modes in biomolecules are coupled with functionally imporant conformational dynamics. Much beyond that, solvent molecules play crucial role in molecular recognition, specificity and stability of folded proteins and IDRs. While in cytoplasm, protein hydration layers have a dynamic equilibrium with bulk. Hence,  we are interested in probing the correlation between internal collective dynamics of proteins and dipolar solvent's collective excitations that paves the way to decipher the underlying normal modes of proteins that hydration layer inherits.