Elucidation of molecular mechanism of polyglutamine protein induced dysfunction of mitochondrial membrane and dynamics

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Polyglutamine disease is neurodegenerative disorder caused by protein misfolding and aggregation. In this study, we analyzed the effect of conformational change of model polyglutamine protein to its enzymatic function and interaction with model lipid membrane. We show the enzymatic activity of polyglutamine protein is suppressed by soluble amyloidogenic conformer. This finding indicates that conformational transitions of polyglutamine protein inhibit physiological function and induce cellular dysfunction.