"Large-Scale Proteomic Analysis of the Effects of Metal-Protein Interactions and Development of Methionine-Based Protein Folding Stability Analysis"
Metal-protein interactions are extensively found throughout biology. However, there are detrimental effects when strictly regulated metal homeostasis is disturbed. One mechanism attributed to metal toxicity, specifically copper, is protein aggregation and precipitation. Metal cations have been exploited for their protein precipitation properties in a wide variety of areas but despite widespread recognition of this phenomenon, the mechanisms of metal-induced protein aggregation have not been fully elucidated nor the susceptibility of individual proteins to aggregation upon exposure to copper ions (Cu). The work in this dissertation is focused on the identification and characterization of proteins throughout proteomics that are sensitive and tolerant to Cu-induced precipitation and on understanding the mechanism behind copper-induced protein precipitation.
