1) The active site of lysozyme comprises of two amino acid residues necessary for catalysis: Glu35 and Asp52. The pka values of the carboxyl side chains of these low residues are 5.9 and 4.5 correspondingly.
a) Describe the ionization state (protonated or deprotonated) of each residue at pH5.2? Determine the pH optimum of lysozyme?
b) describe how can the ionization states of these residues describe the pH-activity profile of lysozyme?