Shown below is a binding curve for a ligand binding to a single binding site on a protein.

From this curve estimate the equilibrium dissociation constant (K_d) for this protein-ligand interaction.

A protein binds to a single small molecule ligand. When the protein (50 pM) is mixed with the ligand (4 nM) and the solution is allowed to reach equilibrium, the proportion of protein molecules bound to the ligand is 10%.

From this single data point, estimate the equilibrium dissociation constant (K_d) for this interaction.

Type the answer as a number in units of nM but do not type the units or any other additional characters (e.g., type 10 rather than 10 nM).

Shown below is a binding curve for a drug binding to a single binding site on a target protein.

From this curve estimate the fraction of protein molecules that will be bound to the drug when the concentration of the drug added to the solution is 80 nM.

Your answer should be given as a number, e.g., 0.5, not 50% (do not type any additional characters)

A protein binds to a small molecule ligand with an equilibrium dissociation constant (K_d) of 0.5 μM.

In a sample containing the protein (10 pM) and the small molecule ligand (50 nM), what proportion of the protein molecules will be bound to the small molecule ligand at equilibrium?

Three different mutant forms of myoglobin bind to oxygen with different affinities.

Their rank order of oxygen affinity is (from strongest to weakest):

Mutant Y > Mutant Z > Mutant X

The oxygen binding curves for these mutants are shown below.

Which curve corresponds to which mutant?

A protein binds to a single small molecule ligand. When the protein (50 pM) is mixed with the ligand (70 nM) and the solution is allowed to reach equilibrium, the proportion of protein molecules bound to the ligand is 99%.

From this single data point, estimate the equilibrium dissociation constant (K_d) for this interaction.

Type the answer as a number in units of nM but do not type the units or any other additional characters (e.g., type 10 rather than 10 nM).

Shown below is a binding curve for a ligand binding to a single binding site on a protein.

From this curve estimate the equilibrium dissociation constant (K_d) for this protein-ligand interaction.

Shown below is a binding curve for a drug binding to a single binding site on a target protein.

From this curve estimate the fraction of protein molecules that will be bound to the drug when the concentration of the drug added to the solution is 30 nM.

Your answer should be given as a number, e.g., 0.5, not 50% (do not type any additional characters)

In the course of their investigations into cancer cell growth, a team of pharmaceutical researchers has discovered a critical oncoprotein (a protein that promotes cancer cell growth).

Now they have developed a new drug that binds to a single site on the oncoprotein with an equilibrium dissociation constant (K_d) of 1 nM.

What concentration of the drug would they need to mix with the oncoprotein so that 99% of the oncoprotein molecules will be bound to the drug?

A heterodimeric protein is composed of two subunits that have similar structures. Each subunit is able to bind to the same ligand molecule. Binding of the ligand to one subunit induces a conformational change in the protein such that the affinity of the ligand for the second subunit increases.

Which of the following binding curves is/are likely to represent this type of protein-ligand interaction?