Thermal stress is the most common stress condition utilized for gauging protein stability, however, melt curves from a protein under different conditions can appear very different but still produce the same Tm from a derivative plot. Microfluidic Modulation Spectroscopy (MMS) is an automated mid-IR technique capable of measuring protein secondary structure at very high resolution across a broad range of concentrations and buffer conditions. MMS can be used to measure and monitor the structural changes that are occurring, leading to protein unfolding, and then thermally induced aggregation. With MMS we can monitor the loss of native protein secondary structure elements as the protein is being subjected to thermal stress. We looked at thermal unfolding for lysozyme across a range of pHs and found the Tm to be pH dependent. We looked at an IgG across a range of concentrations and found the Tm to be modestly concentration independent. Additionally, we used MMS to compare temperature and pressure stress applied to ovalbumin and found that each stress unfolds ovalbumin differently.