Proteins fold into appropriate configuration, called native structure, in order to achieve its cellular function. A protein with nonnative structure induces malfunction and causes the relevant disease. Such protein misfolding has been revealed as a common pathogenic process in many neurodegenerative diseases like Alzheimer's and Parkinson's disease. In Parkinson's disease (PD), a protein called α-synuclein (αS) is found a major component of Lewy body, a proteinaceous aggregate with amyloid

more »

... l form of αS. Considering its character as an intrinsically unfolded protein, the overall change of conformation during PD is quite attractive for biophysicist to understand protein folding and misfolding, and the detailed information can lead to a therapeutic achievement for the treatment of PD. CROSS-β SHEET CORE OF α-SYNUCLEIN AMYLOID FIBRIL DETERMINED BY HYDROGEN/DEUTERIUM EXCHANGE.