Abstract
Misfolding and aggregation of α-synuclein are linked to many neurodegenerative disorders, including Parkinson’s and Alzheimer’s disease. Despite intense research efforts, detailed structural characterization of early conformational transitions that initiate and drive α-synuclein aggregation remains elusive often due to the low sensitivity and ensemble averaging of commonly used techniques. Single-molecule Förster resonance energy transfer (smFRET) provides unique advantages in detecting minor conformations that initiate protein pathologic aggregation. In this chapter, we describe an smFRET-based method for characterizing early conformational conversions that are responsible for α-synuclein self-assembly and aggregation.
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Acknowledgments
This work was supported by laboratory startup funds from the Baylor College of Medicine (A.C.M.F. and J.C.F.). The authors declare no competing financial interests.
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Moosa, M.M., Ferreon, J.C., Ferreon, A.C.M. (2019). Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation. In: Bartels, T. (eds) Alpha-Synuclein. Methods in Molecular Biology, vol 1948. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9124-2_17
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DOI: https://doi.org/10.1007/978-1-4939-9124-2_17
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