Date: October 29th 2019 (Tuesday)
Time: 4:00 PM
Venue: Committee Room (MS710), Chemistry Department, 6th Floor
Abstract: Natively unfolded or intrinsically disordered proteins (IDPs) challenge the traditional sequence-structure-function paradigm and constitute one of the major classes of molecular workhorses. Unlike the folded (globular) proteins, IDPs lack the ability to undergo autonomous folding, exist as dynamic ensembles and underscore the importance of conformational plasticity and heterogeneity in the protein function. However, the disorder-to-function relationships are poorly understood. Additionally, the dysfunction of many IDPs is associated with a range of deadly diseases such as Alzheimer's and Parkinson's diseases and cancers. My laboratory has been investigating the structural and dynamical characteristics of a wide range of disease-associated IDPs that are capable of transforming into highly ordered amyloid assembles. I will describe our recent results that shed lights into the unusual phase behavior of IDPs that undergo liquid-liquid phase separation leading to the formation of liquid droplets that can eventually undergo liquid-to-solid phase transition into more ordered aggregates. We utilized a wide range of multidisciplinary tools to study the fundamental physicochemical factors that govern the phase separation and aggregation. Our studies illuminate the key molecular drivers of IDP phase transition that is involved in both function and disease.