The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What...

The active site of lysozyme contains two amino acid residues essential for catalysis: Glu³⁵
and Asp⁵². The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state
(protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below?