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 (L_{0}), and
[ML] as a function of L or Lo ([ML] = [M_{0}][L]/(KD+ [L]) (when
Lo >> Mo or when free [L] is known) and Y = fractional
saturation = Y = ([ML]/[M_{0}] = [L]/(K_{D}+ [L])
 decide which of two given equations for [ML] should be used
under conditions when the above conditions for L_{0} and L are
given
 based on the equation ([ML] = [M_{0}][L]/(K_{D}+ [L]) draw
qualitative graphs for different given L_{0}, L, and Kd values
 determine fraction saturation given relatives values of Kd
and L, assuming L_{0} >> M_{0}
 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 L_{0}
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
