BIOC 2300BIOC 2610CHEM 2401CHEM 2402
Explain how enzymes can increase the rates of biochemical reactions at the molecular level, and how they may be inhibited or regulated by drugs and toxins. [BIOC 1040] [BIOC 2300] Identify general features of the common classes of biomolecules: carbohydrates, lipids, nucleotides and amino acids. [BIOC 1040] [BIOC 2300] Describe and interrelate the hierarchical levels of protein structure (1˚ to 4˚) and provide examples of how this structure relates to the function (or dysfunction) of various classes of proteins. [BIOC 1040] [BIOC 2300] Predict the fate of a protein based on features of the primary sequence. [BIOC 3400]
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.
