Abstract:

Protein folding is an essential process for both basic biology and biotechnology. Impaired folding of a protein will pose barriers to its engineering and utility; misfolding is also associated with numerous diseases. My research group builds tools to study protein (mis)folding through high throughput frameworks and applies these tools to identify agents that promote the folding or inhibit the misfolding of a target protein. I will describe our work using genetically encoded biosensors to study the aggregation of amyloidogenic proteins and to identify both cyclic peptides and antibody mimetics that bind to different species generated in the amyloid aggregation cascade. I will also discuss our recent efforts to study and engineer the chaperones responsible for the biogenesis of Rubisco, the enzyme responsible for catalyzing carbon dioxide fixation in photosynthetic organisms.