%0 Journal Article %A Ghosh, Dhiman %A Mondal, Mrityunjoy %A Mohite, Ganesh M. %A Singh, Pradeep K. %A Ranjan, Priyatosh %A Anoop, A. %A Ghosh, Saikat %A Jha, Narendra Nath %A Kumar, Ashutosh %A Maji, Samir K. %D 2013 %T The Parkinson’s Disease-Associated H50Q Mutation Accelerates α‑Synuclein Aggregation in Vitro %U https://acs.figshare.com/articles/journal_contribution/The_Parkinson_s_Disease_Associated_H50Q_Mutation_Accelerates_Synuclein_Aggregation_i_in_Vitro_i_/2368417 %R 10.1021/bi400999d.s001 %2 https://acs.figshare.com/ndownloader/files/4007869 %K H 50Q %K Syn %K mutation %K PD %K aggregation %K Parkinson %X 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 in vitro 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. %I ACS Publications