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B. Sc. Biochemistry & Molecular Biology
  • 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.
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