Elizabeth Rhoades, Ph.D., is Associate Professor of Chemistry at the University of Pennsylvania.
A chief interest of the Rhoades research lab lies in discovering principles that govern the functions of intrinsically disordered proteins (IDPs) and why these proteins are so frequently associated with disease. To do this, the Rhoades team uses single-molecule fluorescence and other biophysical techniques to study protein conformations and dynamics, protein-protein interactions, and protein-membrane interactions. Proteins of interest to her group include tau, α-synuclein, islet amyloid polypeptide, and troponin. Single molecule fluorescence – applied to protein molecules that are either diffusing freely through solution (using confocal microscopy) or those localized to a surface (using total internal reflection microscopy) – is one of the Rhoades lab key approaches to studying biological molecules and processes.
Keywords: intrinsically disordered proteins, protein conformation, protein dynamics, protein-protein interactions, protein-membrane interactions, single-molecule optical techniques, tau, α-synuclein, islet amyloid polypeptide, troponin
Working Group(s): Working Group 1: How do cells sense their mechanical environment?