Ataxin-3 misfolding and aggregation process is responsible of a pathological condition known as Spinocerebellar Ataxia-3, a polyglutamine inherited neurodegenerative disease.The pathology is characterized by progressive challenges in movement and balance.This disorder is associated with mutations at the ATAXN3 gene, located to chromosome 14q32.1, that result in the expansion of the Polyglutamminic tail (PolyQ) in the encoded At-3 protein.Extensive research is conducted on protein aggregation pathway, although the underlying molecular mechanisms are not understood yet.In general variation in pH, temperature and interactions with specific properties substrates can influence protein misfolding. Previous studies demonstrate how At-3-N-terminal region called Josephin Domain(JD) has a leading role in At-3 fiber formation for its amyloidogenic propensity.Therefore, understanding the connection between JD structural characteristics and aggregation tendency could enhance the knowledge of the pathology and facilitate the development of a cure. Experimental techniques are not able to simultaneously achieve high resolution on spatial and temporal scales, being limited in their understanding of the dynamics at molecular scale.