Infrared absorption spectroscopy is a powerful analysis tool to study the secondary structure of proteins and their denaturation. The most prominent absorption band of proteins in the mid-IR spectrum is the amide I band (1600-1700 cm–1) which is induced by vibrations of the peptide group and allows the evaluation of the secondary structure. In this spectral region, the most significant difficulty of IR investigations of proteins in aqueous solution is the strong absorbance of the HOH-bending band that overlaps with the amide I band. The use of external-cavity quantum cavity lasers (EC-QCL) facilitates the use of longer path lengths and hence enables more robust measurements even at lower concentrations. At room temperature bovine serum albumin (BSA) displays an alpha helical structure and with increasing temperature the formation of parallel and antiparallel beta sheets takes place. Infrared spectroscopy is sensitive towards beta sheet secondary structure, linked to aggregate formation and is seen as a decrease in the height of the amide I band at wavenumber 1656 cm-1 and the appearance of two bands at 1619 cm-1 and 1692 cm-1 respectively. The temperature at which this occurs changes with the concentration of protein. Another factor that has been shown to affect the stability of proteins is the presence of sugars and various sugars like sucrose, trehalose etc. have been used in the protection of proteins while freezing and during preservation. In this work, a commercially available EC-QCL based mid-IR transmission spectrometer was used to monitor dynamic changes in protein conformation in two and three component solutions exposed to thermal perturbation. First, the concentration of protein in aqueous solutions of protein was varied to study the effect of protein concentration on the onset temperature of thermal denaturation. The concentration of alfa and beta components was measured as the solution was gradually heated from 25°C to 85°C. The inflection point of the concentration versus temperature plot for the alfa helix and beta sheets was taken as the onset temperature for denaturation. The effect of two disaccharides, sucrose and trehalose, and one monosaccharide, mannose, on the denaturation temperatures for BSA was then studied. Initially the concentration of BSA was varied keeping the concentration of sugar in the solution constant and then the molar ratio of sugar to protein in solution was varied. Differences between denaturation temperature as low as 1°C could be observed as distinct differences in spectra in the initial experiments with varying concentration. The expected increase in denaturation temperature with the addition of sugar was also apparent and in addition, the comparison of efficiency of different sugars in stabilizing proteins by delaying denaturation was possible. Hence the capability of mid IR laser based spectroscopy in studying protein denaturation in simple and more complex solutions upto temperatures of upto 85°C was demonstrated. The method shows promise for the food and medicine industry as a possible way to study the efficiency of different stabilizing agents for proteins.