Thesis Abstract

Protein misfolding diseases, such as Alzheimer's disease, Parkinson's disease, and prion diseases, are characterized by the accumulation of misfolded proteins and the formation of toxic aggregates. The biochemistry underlying protein misfolding and aggregation is complex and not fully understood. This project aims to analyze the biochemistry of protein misfolding diseases by investigating the mechanisms of protein misfolding, the role of chaperones and proteases in protein quality control, and the pathways leading to protein aggregation and toxicity. The findings from this study will contribute to a better understanding of the biochemical basis of protein misfolding diseases and may provide insights for the development of therapeutic interventions.

Thesis Overview