• Account for why a given ligand may be bound tightly by an enzyme or covalently modify an enzyme (transition state analogues).
  • Explain how given techniques (spectroscopy, radioactivity, HPLC) may be used to measure enzyme activity in direct or indirect assays.
  • Given a pH-dependent kinetic mechanism, derive an initial velocity equation and sketch the plot of kinetic constants as a function of pH.
  • Given the kinetic mechanism (with or without inhibition), derive an initial velocity equation using either the steady-state assumption or the rapid equilibrium approach.
  • Show how entropic contributions lead to huge intramolecular rate enhancements.
  • Given the kinetic parameters for an enzyme-catalyzed reaction and the corresponding nonenzymatic reaction, calculate the efficiency, rate enhancement, proficiency, and extent of transition state stabilization.
  • Given the steady-state velocity expression for a multisubstrate enzyme, predict the product inhibition pattern and binding order in the presence of fixed and variable substrate concentrations.
  • Derive the steady-state velocity equation for a given kinetic mechanism for a multisubstrate enzyme using the King-Altman method.
  • Identify uniform and differential binding from site-directed mutagenesis studies or substrate mutilation studies to discern the role of residues in transition state and ground state binding.
  • Given an enzyme mechanism, design a reversible or irreversible inhibitor.
  • Given an irreversible inhibitor, design an experiment to determine the efficiency of inactivation and the binding affinity.