New approaches for studying the structure of protein oligomers in lipids and in solutions
Understanding the interaction between membranes and amyloid protein oligomers is a key unsolved challenge in the field of biophysics. Here we describe new tools to address this challenge. We show that single molecule photobleaching with a home-built Total Internal Reflection Fluorescence Microscope can measure the relative membrane affinity of each type of oligomers. Also, an Atomic Force Microscope coupled to a home-built Confocal Fluorescence Microscope can probe the membrane phase dependant binding of these oligomers. Separately, fiber-optic in-probe modulation of pH during an NMR experiment can potentially probe the evolving oligomeric structure.