Exploring/Improving 3D Protein Shape and Dynamics in the Cell with Lasers, LEDs, Magnets and Electron Beams

Welcome to the world of high resolution molecular spectroscopy and protein folding/aggregation in the cell!

The Cavagnero lab develops novel approaches employing lasers, LEDs and magnets to increase the performance of nuclear magnetic resonance (NMR) spectroscopy for the structural and dynamic characterization of biomolecules by photochemically induced dynamic nuclear polarization and other hyperpolarization techniques. We are also extremely interested in understanding how proteins achieve their 3-dimensional shape within the cellular context in the presence of the ribosome and molecular chaperones.  Towards this end, we use a variety of chemical-biology and spectroscopic techniques including genetic recombineering, unnatural tRNA and cell-free technologies, time resolved fluorescence depolarization, single-molecule fluorescence spectroscopy/microscopy, and multidimensional NMR.  Understanding how to more efficiently determine biomolecular structure and dynamics and how to unveil the principles governing protein 3D shape formation (folding) in the cell will provide key insights into the fundamental nature of life and evolution.  Importantly, our work will provide essential information to more efficiently manufacture protein-based pharmaceuticals in biotechnology, and to devise better approaches to cure deadly misfolding-based diseases.