Washington University in St. Louis (WU)
My area of research pertains identifying the mechanisms of (dys)function of intrinsically disordered proteins. To this end we use a combination of single-molecule spectroscopy (in vitro and in cell), ensemble methods, and theoretical modeling to identify how disordered proteins achieve their functional role. Systems of interest in the lab includes: i) Apolipoprotein E: we demonstrate that the protein is more dynamic than what was previously determined with traditional techniques of structural biology, offering a readout to identify possible effectors of its structure, ii) the polypyrimidine tract binding protein, which accumulates in a class of membraneless condensates called perinucleolar compartments (a target for cancer therapy); iii) the nucleocapsid protein of SARS-CoV-2, which regulates the condensation of the viral genome.