Question #112133

The tertiary structure of a monomeric enzyme is critically stabilized by a single electrostatic salt bridge between the side chains of an Aspartic acid residue ($pK_{aR} = 3.90$) and a Histidine residue ($pK_{aR} = 6.10$). The enzyme undergoes pH-induced denaturation when this salt bridge is disrupted. The salt bridge is considered intact only when the Aspartate side chain is fully deprotonated and the Histidine side chain is fully protonated. Assuming the given $pK_{aR}$ values are the effective constants in the folded state and their ionizations are statistically independent, determine the maximum percentage of the enzyme in the native (folded) state at $298\text{ K}$, and the optimal pH for this stability, respectively.\n\n(Given: $10^{1.1} = 12.59$)