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Methods Mol Biol. 2019;1948:221-233. doi: 10.1007/978-1-4939-9124-2_17.

Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation.

Author information

1
Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX, USA.
2
Department of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX, USA. allan.ferreon@bcm.edu.

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.

KEYWORDS:

Facilitated self-assembly; Intrinsically disordered protein; Neurodegenerative disease; Protein aggregation; Single-molecule spectroscopy

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