Seminar Abstract:  The misfolded proteins associated with neurodegenerative disease can adopt a variety of different conformations, some of which are toxic. Because these proteins have identical amino acid sequences, the cellular environment clearly influences the final state, yet most structural studies do not include the cellular context and, perhaps because we are not studying the correct conformation, not a single therapeutic strategy for these diseases addresses the underlying protein misfolding pathology. Using new sensitivity-enhancement technology for solid state NMR spectroscopy, Dynamic Nuclear Polarization, we study protein structure in native environments - inside living cells - to reveal how both healthy and disease-relevant cellular environments influence protein structure.

Originally published at chemistry.nd.edu.