Abstract
Using small fragments, formed by proteolysis, of the intrinsically disordered protein tau, we identified a region of the protein that is crucial for forming amyloid fibers. The fibers formed by the selected region of tau were capable of propagating, and seeding the aggregation of additional naive tau species. Additionally, using double electron-electron resonance (DEER), a pulsed EPR technique, we measured distinct fibril conformations populated by these new fibers.
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