The Parkinson’s Disease-Associated H50Q Mutation Accelerates α‑Synuclein Aggregation <i>in Vitro</i> Dhiman Ghosh Mrityunjoy Mondal Ganesh M. Mohite Pradeep K. Singh Priyatosh Ranjan A. Anoop Saikat Ghosh Narendra Nath Jha Ashutosh Kumar Samir K. Maji 10.1021/bi400999d.s001 https://acs.figshare.com/articles/journal_contribution/The_Parkinson_s_Disease_Associated_H50Q_Mutation_Accelerates_Synuclein_Aggregation_i_in_Vitro_i_/2368417 α-Synuclein (α-Syn) aggregation is directly linked with Parkinson’s disease (PD) pathogenesis. Here, we analyzed the aggregation of newly discovered α-Syn missense mutant H50Q <i>in vitro</i> and found that this mutation significantly accelerates the aggregation and amyloid formation of α-Syn. This mutation, however, did not alter the overall secondary structure as suggested by two-dimensional nuclear magnetic resonance and circular dichroism spectroscopy. The initial oligomerization study by cross-linking and chromatographic techniques suggested that this mutant oligomerizes to an extent similar to that of the wild-type α-Syn protein. Understanding the aggregation mechanism of this H50Q mutant may help to establish the aggregation and phenotypic relationship of this novel mutant in PD. 2013-10-08 00:00:00 H 50Q Syn mutation PD aggregation Parkinson