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Here, \u03b1\u2010synuclein conformers are characterized by analysis of the charge\u2010state distributions observed in electrospray\u2010ionization mass spectrometry under negative\u2010ion mode. It is found that, even at neutral pH, a small fraction of the molecular population is in a compact conformation. Several distinct partially folded forms are then identified under conditions that promote \u03b1\u2010synuclein aggregation, such as solutions of simple and fluorinated alcohols. Specific intermediates accumulate at increasing concentrations of ethanol, hexafluoro\u20102\u2010propanol, and trifluoroethanol. Finally, extensive folding induced by Cu<jats:sup>2+<\/jats:sup> binding is revealed by titrations in the presence of Cu<jats:sup>2+<\/jats:sup>\u2013glycine. The data confirm the existence of a single, high\u2010affinity binding site for Cu<jats:sup>2+<\/jats:sup>. Because accumulation of this partially folded form correlates with enhancement of fibrillation kinetics, it is likely to represent an amyloidogenic intermediate in \u03b1\u2010synuclein conformational transitions. Proteins 2011. \u00a9 2010 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.22909","type":"journal-article","created":{"date-parts":[[2010,10,12]],"date-time":"2010-10-12T22:38:11Z","timestamp":1286923091000},"page":"611-621","source":"Crossref","is-referenced-by-count":51,"title":["Compact conformations of \u03b1\u2010synuclein induced by alcohols and copper"],"prefix":"10.1002","volume":"79","author":[{"given":"Antonino","family":"Natalello","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Federico","family":"Benetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia 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