Determining protein structure is of extreme importance as it pertains to drug development, discovery of protein function, and identifying disease states in cells. Similarly, identifying different conformational changes proteins experience plays a role in all the previously mentioned disciplines as well as how the cell recognizes and reacts to these altered proteins. Protein structure and subsequent conformational changes can be determined with a high degree of accuracy through methods such as X-ray crystallography, Cryo-EM, and NMR. However, these methods are time consuming, difficult, and require expensive equipment. Here, we aim to develop a lower resolution Intrinsic Tryptophan/Tyrosine Fluorescence (ITF) based method to determine changes in protein structure due to oxidation and relate this to how proteins are selectively digested. Bovine Serum Albumin (BSA) has been used as our model protein to determine changes in protein structure. Our results show that hydrogen peroxide treated BSA has a concentration dependent change in ITF compared to non-treated BSA. This suggests that oxidized BSA undergoes a conformational change that alters the exposure of its tryptophan and tyrosine residues to the solvent. For this presentation, I will discuss my work using ITF as a fast, easy, low-resolution method to probe structural changes in BSA and other proteins exposed to various conditions.