Date: April 08th 2019 (Monday)
Time: 4 PM
Venue: Committee Room (MS710), Chemistry Department, 6th Floor
Abstract: Natively unfolded or intrinsically disordered proteins (IDPs) challenge the traditional sequence-structure-function paradigm. 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, disorder-to-function relationships are poorly understood. Additionally, the aberrant phase transition 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 key structural and dynamical characteristics of a wide range of disease-associated IDPs that are capable of transforming into highly ordered nanoscopic amyloid assembles. We are particularly interested in elucidating the fundamental molecular determinants that dictate the complex interplay of chain-chain and chain-solvent interactions resulting in aggregation and phase separation of IDPs. 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 mesoscopic liquid droplets that can eventually mature into more ordered aggregates. .