The h50q mutation induces a 10-fold decrease in the solubility of α-synuclein*

HIGHLIGHTS

• who: Riccardo Porcari from the In conclusion, we have presented an analysis of the modulation of the aggregation process of the H Q variant u2423-Syn by the WT form and of the features in their sequence and structure that are associated with their different aggregation behaviorOur results show that the changes in the ratio between the concentrations of the WT and H Q u2423-Syn, in the secondary structure populations of the monomeric ensemble, and in the thermodynamic stability of the fibrils, are closely associated with an alteration of the aggregation behavior of this protein. Acknowledgments . . .
  

   

  

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