My lab is primarily involved with the application of NMR spectroscopy to problems in non-native structural biology. This includes characterizing the location and extent of structure in and the intermolecular interactions of aggregation-competent partially unfolded states of proteins involved in neurodegenerative disease. Specific targets include Alzheimer's Disease and Parkinson's Disease related proteins. We are also pursuing structural characterization of lipid-induced conformational changes of these proteins.
A related area of interest is the study of partially folded equilibrium states with high fidelity to intermediates observed during protein folding kinetics. Optical probes and measurements of backbone amide proton protection are used to establish this congruence. Direct NMR studies of the equilibrium states result in detailed structural insights into structure formation during protein folding.