Reports and Figures.

A. Lysozyme Extraction, Purification and Crystallization from Hen Egg White

Figure 4: PyMOL image of D48A mutated egg hen lysozyme bounded to (GlcNAc)4 Image 4a shows the overall lysozyme enzyme structure with positive side chains labeled in green and negative side chains labeled in dark blue. As well, (GlcNAc)4 (also known as NAG) is colored in red. Side chains responsible for forming 6 hydrogen bonds (shown in yellow dashes) toward the NAG ligand is shown in figure 4b along side two important catalytic residues: Asp52 (orange) and Glu35 (magenta). Trp62 is depicted in teal and shown in image 4c stacked with the glucose-like ring in the (GlcNAc)4 ligand. White dashes illustrate the parallel nature of this arrangement.
Figure 5: PyMOL image of D48A mutated egg hen lysozyme compared in the presence and absence of ligand (GlcNAc)4 The superimposed figure of D48A lysozyme in the presence and absence of ligand (GlcNAc) 4 can be observed in 5a. Enzyme in green shows the conformation without ligand and magenta depicts the enzyme with ligand binding. In 5b, two side chains from the bound conformation and unbound conformation are compared. The Asp101 residue can be recognized moving 4 angstroms towards the ligand and the Asn59 residue moved 2.4 angstroms (measurements depicted in yellow dashes).

B. Alkaline Phosphatase Enzyme Kinetics

C. Investigation into the Structural, Functional and Clinical Implications of the Hemoglobin with Wild Type HbA