title: Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence.
abstract: The aggregation and deposition of the neuronal protein α-synuclein in the substantia nigra region of the brain is a key pathological feature of Parkinson's disease. α-Synuclein assembles from a monomeric state in solution, which lacks stable secondary and tertiary contacts, into highly structured fibrillar aggregates through a pathway which involves the population of multiple oligomeric species over a range of time scales. These features make α-synuclein well suited for study with single-molecule techniques, which are particularly useful for characterizing dynamic, heterogeneous samples. Here, we review the current literature featuring single-molecule fluorescence studies of α-synuclein and discuss how these studies have contributed to our understanding of both its function and its role in disease.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06511, USA.
authors.forename: Adam J
authors.initials: AJ
authors.lastname: Trexler
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Rhoades
mesh_terms: D000818:Animals; D006801:Humans; D011487:Protein Conformation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence / Q000379:methods; D013329:Structure-Activity Relationship; D051844:alpha-Synuclein / Q000737:chemistry* / Q000502:physiology*
chemical_list: D051844:alpha-Synuclein