Albumin is one of the most studied proteins because of its diverse functions (Peters, 1995). Albumin varies between species, but past research on Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) has shown structural similarities between the two. Binding properties of HSA and BSA can be compared using the thermodynamic parameters of enthalpy, entropy, and Gibbs free energy (ΔH, ΔS, and ΔG). Previous studies have shown a linear relationship between enthalpy and entropy when temperature is held constant (enthalpy-entropy compensation). Prior data used thermodynamics to compare the two proteins on a micro-level (1-10 ligands). This thesis is the first to statistically analyze thermodynamic quantities in the binding of ligands to HSA and BSA on a macro-level (200+ ligands). A bioinformatic approach was used to obtain thermodynamic data from 197 primary literature sources available in PubMed (Sayer, et al., 2022). Linear regression was applied and showed a significant positive correlation between enthalpy and entropy in both proteins examined. The findings indicate the existence of a significant enthalpy-entropy compensation. This thesis quantitatively described the variation of ΔH°, ΔS°, ΔG° in the binding of ligands to BSA and HSA by using Cumulative Distribution Function (CDF). The obtained CDFs were used to derived Normalized Probability Density Function (NPDF) for each thermodynamic quality. The Shannon entropy was calculated to assess the variability on ΔH°, ΔS°, ΔG°. The resulting values of Shannon entropy shows that both ΔH° and TΔS° have larger values than that of ΔG° for both proteins. ΔG° contained lower levels of information (uncertainty) than ΔH° and TΔS° for both proteins. Keywords: Bovine Serum Albumin; Human Serum Albumin; Thermodynamics; Enthalpy; Entropy;