Current Crosslistings BIOC 5701
BIOC 5701
BIOC 3700
Determine the effects of loss of function or gain of function mutations of regulating enzymes or metabolic enzymes on the rate of a reaction given a schematic of enzyme regulation. [BIOC 2300] Given the substrates, products, and cofactors for a particular class of enzyme-catalyzed reaction, write a mechanism for the reaction. [BIOC 3700]
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.
