Correlation of Amyloid Fibril β‐Structure with the Unfolded State of α‐Synuclein

Many neurodegenerative disorders are associated with the deposition of amyloid fibrils. Aggregation is generally initiated by unfolding of the native state of the aggregating protein, then conversion into a β-sheet-rich architecture. Using solution- and solid-state NMR spectroscopy, we show that the secondary structure of α-synuclein fibrils, the major component of deposits in Parkinson's disease, correlates directly with the structural properties of the unfolded state.