Abstract
Protein aggregation is associated with various neurodegenerative diseases, including Huntington's disease, where a CAG-repeat expansion leads to huntingtin (htt) proteins with extended, aggregation-prone, polyglutamine (polyQ) tracts. The aggregation of these proteins leads to amyloid fibrils with a pronounced beta-sheet content. The exact underlying mechanisms of htt/polyQ aggregation remain poorly understood. in this work, we present a coarse-grained molecular dynamics study on the aggregation of polyQ into amyloid-like structures.
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