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1. Enzymatic Catalysis

   Linked via "hydrophobic packing"

   The core principle of enzymatic catalysis aligns with general chemical kinetics: lowering the $\text{E}_a$ allows a greater fraction of substrate molecules to overcome the energy barrier at physiological temperatures, thus increasing the reaction velocity ($v$). In the simplest Michaelis-Menten model, the formation of the enzyme-substrate complex ($\text{ES}$) is the initial, rapid step:
   $$\text{E} + \text{S} \rightleftharpoons \text{ES…