Prof. Martin Zanni, University of Wisconsin-Madison

New technology for 2D IR spectroscopy and its application to protein aggregation and drug binding

Physical Chemistry Seminar Series

In just the last couple of years, 2D IR spectroscopy has evolved into a useful tool in the chemical, biological and energy sciences. In this talk, I will describe experiments in which we have used 2D IR spectroscopy and isotope labeling to determine, with residue-specificity, the binding mechanism and structure of an amyloid inhibitor that prevents the formation of amylin amyloid fibers, which is the polypeptide associated with type 2 diabetes. I will also present work in which we have used expressed protein ligation to uniformly isotope label an entire domain of a crystallin protein involved in cataract formation, from which we study its aggregate structure and kinetics. Finally, I will present a recent technological development that paves the way to commercialization of a 2D IR spectrometer.

For more information contact Prof. Christine Payne (404-385-3125).