Discriminate between and calculate the roles of entropy, enthalpy, and molecular interactions in protein stability, folding and ligand binding.Given the architecture of an enzyme active site, write a mechanism and show how general acid/base, covalent, or electrophilic catalysis may occur.Given the kinetic mechanism (with or without inhibition), derive an initial velocity equation using either the steady-state assumption or the rapid equilibrium approach.Draw the structure of a peptide with defined stereochemistry at a given pH.Given the substrates, products, and cofactors for a particular class of enzyme-catalyzed reaction, write a mechanism for the reaction.Analyze implications of molecular spectroscopy (absorption, emission, CD, NMR) results on polypeptide structure and environment in direct context of the physical basis of the technique in question.Given an enzyme mechanism, design a reversible or irreversible inhibitor.Apply peptide bond properties and hydrogen-bonding to predict primary and secondary structuring preferences.