Abstract by Nathan Zuniga
Chemistry and Biochemistry
Protein Stability: Determining C1/2 via Chemical Labeling Method
Recent studies demonstrate that imbalances in the quality and concentration of most proteins in each cell (proteostasis) are at the core of many of today’s devastating diseases. Thus, it is important to create diagnostic methods that can detect changes in the quality and concentration of many proteins within a patient’s proteome. Recent studies suggest that either protein modification or changes in secondary structure could influence disease etiology.Our objective focuses on the use of chemical probes to monitor protein unfolding energies across the proteome by modifying surface exposed AA sites during denaturation. We are optimizing use of tyrosine, tryptophan, and methionine. These modifications are introduced at different degrees of protein unfolding, and measured with mass spectrometry. Use of these three probes should result in the ability to monitor 98% of the proteome. This will allow us to test how protein homeostasis changes with RA development. This understanding will also lead to greater knowledge of the control of protein homeostasis during development and aging.