Research

Our Research

At the Mukhopadhyay Lab, we are interested in uncovering the behavior of Intrinsically disordered proteins or proteins with intrinsically disordered regions (IDRs) that lack a strict three-dimensional structure using a range of biophysical tools. Our lab has primarily been interested in exploring the behavior of amyloid-like aggregates formed by numerous prion-like proteins, in vitro. Recent interest in this class of proteins comes from their ability to undergo the physical process of phase separation, forming liquid-like assemblies that can act as membrane-less subcompartments within a cell. The ability of IDPs to form and sequester other biomolecular components into membrane-less assemblies is critical for their integration into multiple essential biochemical networks and in the maintenance of the cellular landscape. Such assemblies are also crucial in organizing various membrane-bound organelles, such as the nucleus, where they are involved in a wide range of functions, including the formation of a selective permeability barrier on the nuclear envelope that regulates nucleocytoplasmic exchange and in the formation of nucleoli, which act as hubs for ribosome assembly. However, dysregulation and subsequent changes in the material properties of these condensates are associated with several neurodegenerative diseases and cancer, amongst others. Using an array of biophysical, fluorescence-based tools from the ensemble to the single-molecule level and at different time scales, we probe these changes that very often contribute to the pathophysiology of numerous diseases in order to elucidate the molecular determinants of such aberrant changes in the physical properties of the biological condensates and their transition into more solid-like amyloid aggregates.