Examining the Atypical Structure Adopted by the 37-51 Segment of α-synuclein in the Early Stage of Aggregation
The aggregation of -synuclein into insoluble filaments is a hallmark of Parkinsons disease. Upon membrane binding, -synuclein adopts a helical conformation, whereas during neurodegeneration it misfolds and aggregates into {beta}-sheet-rich structures. However, the factors that trigger the misfolding and aggregation remain poorly understood. In this study, coarse-grained molecular dynamics…
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