The immediate goal of this research is to study the thermal unfolding of two biomedically important proteins: apolipoprotein (a) and porcine pancreatic lipase at various pH values, solvent conditions and protein concentrations. Apolipoprotein (a), a cholesterol-ester/LDL-like particle was selected for analysis because it has been found to be highly atherogenic (that is, associated with atherosclerotic cardiovascular disease) and has a fascinating structure composed of 17 almost identical domains. At the carboxy terminus, apolipoprotein (a) has single copies of sequences resembling the protease domain of plasminogen. Apolipoprotein (a) is not commercially available but milligram quantities of it are available to us from a confirmed source. Porcine pancreatic lipase has been selected for analysis because of its function; which is to catalyze the hydrolysis of ester bonds of nonpolar dietary long-chain triglycerides. Students will be trained in protein purification techniques and will (1) purify pancreatic lipase from the pancreas of freshly slaughtered hogs, (2) characterize pancreatic lipase using enzyme assays and biochemical methods and (3) study the nature of the proteins' thermal unfolding using differential scanning calorimetry.