Abstract
Amyloid fibrils are involved in a number of diseases and notably play a role in neurodegeneration, where they are present in plaques in the brain. Their structure determination might help in finding ways to interfere with their formation, and ultimately prevent disease, by revealing the structure-function relationship and hel** to design molecules targeting initial assembly steps and further propagation. Here, we describe the different steps in NMR protocols which allowed the 3D structure determination of amyloid-β fibrils.
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Acknowledgments
The authors thank all students and post-docs who have developed the protocols in the frame of their project in the two labs. This work was supported by the CNRS and the ETH Zurich.
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Meier, B.H., Böckmann, A. (2023). Solid-State NMR Structure of Amyloid-β Fibrils. In: Cieplak, A.S. (eds) Protein Aggregation. Methods in Molecular Biology, vol 2551. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2597-2_5
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DOI: https://doi.org/10.1007/978-1-0716-2597-2_5
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