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.
CITATION STYLE
Moosa, M. M., Ferreon, J. C., & Ferreon, A. C. M. (2019). Single-molecule FRET detection of early-stage conformations in α-synuclein aggregation. In Methods in Molecular Biology (Vol. 1948, pp. 221–233). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9124-2_17
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