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To obtain insight into the properties of \u03b1S in an aggregation\u2010prone state, we studied the structural properties of \u03b1S at acidic pH using NMR spectroscopy and computation. NMR demonstrated that \u03b1S remains natively unfolded at lower pH, but secondary structure propensities were changed in proximity to acidic residues. The ensemble of conformations of \u03b1S at acidic pH is characterized by a rigidification and compaction of the Asp and Glu\u2010rich C\u2010terminal region, an increased probability for proximity between the NAC\u2010region and the C\u2010terminal region and a lower probability for interactions between the N\u2010 and C\u2010terminal regions.<\/jats:p>","DOI":"10.1002\/pro.194","type":"journal-article","created":{"date-parts":[[2009,6,24]],"date-time":"2009-06-24T15:46:15Z","timestamp":1245858375000},"page":"1840-1846","source":"Crossref","is-referenced-by-count":110,"title":["Structural characterization of \u03b1\u2010synuclein in an aggregation prone 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