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.

Note: The content above has been extracted from a research article, so it may not display correctly.



Q&A
Please log in to submit your questions online.
Your question will be posted on the Bio-101 website. We will send your questions to the authors of this protocol and Bio-protocol community members who are experienced with this method. you will be informed using the email address associated with your Bio-protocol account.



We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.