Assuming you have an agonist, a competitive antagonist, and an easy assay for measuring binding of the agonist, describe a simple experiment that would allow you to determine specific binding, nonspecific binding, and total binding of the agonist at a SINGLE concentration.

Mutations in adenylate kinase have led to a hyperactive enzyme that ultimately ends up elevating ADP levels in a cell.Calculate the EC (energy charge) given the following atypical adenylate concentrations for the cell containing the mutant adenylate kinase: ATP = 0.5 ??��, ADP = 12.2 ??��, AMP = 80 ??��.

In pure noncompetitive inhibition:   a. Where on the enzyme does the inhibitor bind?   b. Does the inhibitor bind to E, ES or both?   c. What is the effect of I on Vmax?   d. What is the effect of I on Km?

Briefly explain the difference between a receptor antagonist and a receptor inverse agonist. Describe both the resulting receptor conformation as well as the signal transduction.

Explain the differences and similarities in the three kinds of reversible inhibition.  Include what is physically happening, how inhibition affects KM and Vmax and if the inhibition can be overcome.

From the Hill Plot below, the of the first binding event for the receptor-ligand system under study is: Q1 4nM Ο 10 μΜ -2 nM 2 nM Calculate the Hill Coefficient from the receptor-ligand binding data below: Q2 4 100 2 3 (0-1) 60 log 10 8 6 4 2 0 -2 -4 -6 -6 -4 -2 0 2 4 log [L] (nM) 6 8 10

The name of the enzyme that recognizes phosphotyrosines on an activated tyrosine kinase receptor in the Akt pathway is

Present the comparison of pharmacokinetics vs pharmacodynamics.  Why the identification of different types of receptors is so important for drug’s pharmacodymics?

Explain how mutations in the R or C subunit of cAMP-dependent protein kinase (PKA) might lead to (a) a constantly active PKA or (b) a constantly inactive PKA.

what is the difference between a partial agonist,full agonist and an inverse agonist ,and why they will be difference?