Abstract by Monica Berg
Chemistry and Biochemistry
Protein Stability Data Analysis Workflow Software Development
Proteins are the primary actuators of cellular functions, meaning a loss in proteostasis, caused by abnormal protein concentration and quality, can lead to disease. Protein quality is measured by protein function and ability to perform those functions, in turn determined and therefore measured by protein fold quality. Folding and flexibility changes in a protein change its thermal stability, proportional to the denaturation midpoint C1/2. C1/2 and the folding stability of each protein in a proteome can be measured between experimental conditions (e.g., health/diseases) for thousands of proteins at once through mass spectrometry. However, analysis of these data is slow, highly error-prone, and requires highly specialized training. I will report on our efforts to remove these barriers by creating a user-friendly software that automates analysis and produces comprehensive graphs to help interpret results, both of which it can now do for varying numbers of conditions and replicates.