Research Focus
Liquid-liquid phase separation (LLPS) occurs in living cells, in which liquid-like membrane-less compartments form. These protein enriched biomolecular condensates regulate biochemical and biophysical processes, but have been linked to formation of protein aggregates found in neurodegenerative diseases. LLPS stems from intrinsically disordered proteins (IDPs), where protein-protein interactions between regions of low complexity have been shown to be a major driving force. However, little is known about the role of the water solvent in this process. Why do two coexisting liquid phases that are entropically unfavorable form? How do properties of water inside biomolecular condensates differ from water outside? How do protein-water interactions, i.e. hydration water, contribute to driving LLPS?Our group studies macroscopic and microscopic solvent properties of biomolecular condensate systems. We use linear and nonlinear spectroscopic methods to probe the structure and dynamics of bulk and interfacial water. We aim to understand the underlying thermodynamic properties of protein-water interactions that lead to LLPS.
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