Rahel Lema is a rising sophomore at the University of Maryland, Baltimore County, where she studies Biochemistry and Molecular Biology. She plans on pursuing her Ph.D. in chemistry or biochemistry after completing her undergraduate studies. This summer, she is working in Dr. James Mack’s lab under the guidance of graduate student Jazmine Crain, investigating proteins’ biochemical responses under mechanochemical conditions. Mechanical stress in proteins has gained significant research attention in that prolonged, destabilizing mechanical energy has been identified as a potential factor in the progression of selective neurodegenerative diseases, such as Alzheimer's and Parkinson’s Disease. Researchers have been trying to understand the molecular events of protein unfolding and destabilization via mechanical stress but lack the appropriate tools to do so. Therefore, more information about the response of proteins to mechanical stress is required. We look to employ mechanochemistry as a tool to test the events of protein unfolding. With this, we can directly apply mechanical stress to proteins and track their physiological and structural changes. By using a temperature and oscillation frequency controlled milling system, we are able to observe the degree of energy in which transforms the rheology and function of the protein. To test our method of various mechanical conditions, we choose to work with the model protein BSA (bovine serum albumin). BSA is a protein that is found in plasma and serum, which maintains the pressure and flow of body compartments, as well as several other capabilities. To subject the protein to stress, it is placed along with a 3”16” stainless steel ball at a range of oscillation frequencies in a ball mill. Techniques such as MALDI-MS TOF allow for the detection of structural changes after milling. To measure functional changes, molecular interactions between BSA and the drug warfarin are analyzed through Isothermal Titration Calorimetry (ITC).