Abstract
Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention. An IDP, which plays a crucial role in a variety of neurodegenerative diseases, is the protein Tau. As a microtubule-associated protein, Tau regulates the assembly and dynamics of microtubules. In the brain of Alzheimer disease patients, Tau is hyperphosphorylated and insoluble deposits of Tau correlate with disease progression. Using NMR spectroscopy as the primary tool we have studied the dynamic ensemble of conformations of Tau in solution, the modulation of dynamic Tau structure by phosphorylation, the structure of Tau aggregates, the mechanism of Tau aggregation inhibitors as well as the interaction of Tau with microtubules and molecular chaperones. To this end we developed improved methods for NMR resonance assignment and ensemble determination. In this presentation I will present recent progress in our understanding of the structural polymorphism of Tau.
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