Protein conformational perturbations in hereditary amyloidosis : Differential impact of single point mutations in ApoAI amyloidogenic variants
Amyloidoses are devastating diseases characterized by accumulation of misfolded proteins which aggregate in fibrils. Specific gene mutations in Apolipoprotein A I (ApoAI) are associated with systemic amyloidoses. Little is known on the effect of mutations on ApoAI structure and amyloid properties. Here we performed a physicochemical characterization of L75P- and L174S-amyloidogenic ApoAI (AApoAI)
