Learning Goals/Objectives for Chapter 5A:  After class and this reading, students will be able to

• write equations for the dissociation constant (KD), mass balance of total macromolecule (M0), total ligand (L₀), and [ML]  as a function of L or Lo ([ML] = [M₀][L]/(KD+ [L])  (when Lo >> Mo or when free [L] is known) and Y = fractional saturation =  Y = ([ML]/[M₀] = [L]/(K_D+ [L])
• decide which of two given equations for [ML] should be used under conditions when the above conditions for L₀ and L are given
• based on the equation ([ML] = [M₀][L]/(K_D+ [L]) draw qualitative graphs for different given L₀, L, and Kd values
• determine fraction saturation given relatives values of Kd and L, assuming L₀ >> M₀
• compare relative % bound for covalent binding of protons to an acid and noncovalent binding of a ligand to a macromolecule given pka/pH and Kd/L values
• describe differences in binding curves for binding of a ligand to a macromolecule and the dimerization of a macromolecule
• derive an equation which shows the relationships between the rate constant for binding (k_on), dissociation (k_off) and the thermodynamic dissociation (Kd) or equilibrium constant (Keq).
• describe the structural and mathematic differences between specific and nonspecific binding
• given a Kd, estimate t_1/2 values for the lifetime of the ML complex.
• describe techniques used to determine ML for given L or L₀ values, including those that do and do not require separation of ML from M , so that Kd values for a M and L interaction can be determined
• List advantages of isothermal titration calorimetry and surface plasmon resonance in determination of binding interaction parameters