This in vitro EPR study was performed using full-length Tau in the absence and presence of Hsp90. Spin labeling sites were established before in single-molecule FRET (38, 39). Analysis of the conformational ensemble of Tau was based on EPR dipolar spectroscopy using DEER (3335). Long-range intramolecular distance information was obtained with doubly spin-labeled Tau molecules and supported by monitoring the local side-chain dynamics of singly spin-labeled Tau. In addition, intermolecular interactions were monitored by DEER and singly spin-labeled Tau derivatives to gain insight into the oligomerization state of Tau. Biochemical assays, e.g., sucrose gradient ultracentrifugation, and QCM helped to shape and support the findings.

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