This thesis presents a detailed description and analysis of the circular dichroism studies performed on the aromatic residues of fructose 1, 6-bisphosphatase (FbPase) from turkey liver under various experimental conditions. Circular dichroism studies performed on the aromatic residues of FbPase indicate that the presence of the substrate, fructose 1, 6-bisphosphate (FbP) and/or the allosteric inhibitor, adenosine monophosphate (AMP) as well as changes in the pH of the medium produce significant effects on the conformation of the enzyme. The effect of the inhibitor, AMP, on the conformation of the enzyme is more pronounced than that of the substrate, FbP.