About

Hello! I am Roopali Khanna. I am an Integrated MS-PhD student and a PMRF fellow at the Department of Biological Sciences at the Indian Institute of Science Education and Research, Mohali. I am currently working in the laboratory of Professor Samrat Mukhopadhyay.

During my time as a Master’s student at IISER, I developed a fascination with a class of proteins that lack a fixed three-dimensional structure and challenge the traditional structure-function paradigm of proteins. These Intrinsically disordered proteins (IDPs) make up almost thirty percent of our proteome and are involved in a wide range of critical cellular functions. Unlike other well-celebrated proteins that adopt a fixed three-dimensional structure, IDPs exist as an ensemble of rapidly fluctuating conformations that can interact with multiple molecular partners to function in the cellular milieu. Owing to their inherent sequence characteristics, IDPs can act as drivers for the biophysical process of phase separation, allowing the formation of membraneless compartments within cells. Via this process, cells can selectively partition specific subsets of biomolecules into on-demand, membraneless, dynamic mesoscopic assemblies. Such phase-separated biomolecular condensates are also essential in preserving the precise spatiotemporal patterning of molecules within membrane-bound organelles such as the nucleus, which exists as an immensely dense, viscoelastic network of biomolecules with a functionally relevant, complex structure. These non-canonical nuclear condensates have emerged at the forefront of most nuclear activities and are driven by transient, multivalent interactions amongst intrinsically disordered proteins or regions, both in the absence and presence of nucleic acids.