<h3>Title</h3>
<h3>New approaches for studying the structure of protein oligomers in lipids and in solutions</h3>
<p><strong><span style="text-decoration: underline;">Abstract</span> :</strong></p>
<p style="text-align: justify;">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.</p>