For a binding protein to show positive cooperativity…. Choice 1 of 4:the protein must be able to adopt at least 2 different conformations each with different affinities for the ligand Choice 2 of 4:the protein must be able to bind to at least 2 different types of ligand Choice 3 of 4:the protein must bind to one molecule of ligand fast and one molecule of ligand slowly Choice 4 of 4:the Kd must be in the micromolar range

For a binding protein to show positive cooperativity…. Choice 1 of 4:the protein must be able to adopt at least 2 different conformations each with different affinities for the ligand Choice 2 of 4:the protein must be able to bind to at least 2 different types of ligand Choice 3 of 4:the protein must bind to one molecule of ligand fast and one molecule of ligand slowly Choice 4 of 4:the Kd must be in the micromolar range

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter17: Genes And The Immune System

Section: Chapter Questions

Problem 7QP

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Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.
Three different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?
Protein A binds to Ligand X with a Kd of 1 μM. Protein B binds to Ligand Y with a Kd of 100 nM. Which of the following statements is TRUE? A. Protein A binds Ligand X ten times tighter than Protein B binds Ligand Y B. At a sufficiently high concentration of ligand, the binding becomes irreversible C. When the concentration of Ligand X is 1 μM, 50% of Protein A is bound to ligand D. Protein B binds to Ligand Y with a Kd of 1 × 10-8 mol/L. E. When both binding reactions are at equilibrium, Protein A has more Ligand X bound than Protein B has ligand Y bound The answer is C, could you show how to get the answer? Thanks
Which of the following must be true based on the data below for ligand L binding to protein A and to protein B? Choice 1 of 4:Protein A binds at least 2 molecules of ligand L. Choice 2 of 4:The Kd for ligand binding to B is approximately 4 micromolar. Choice 3 of 4:When exposed to ligand L, protein A reaches maximal binding faster than does protein B. Choice 4 of 4:Protein B must adopt at least 2 different conformations with different binding affinities.
For a protein that binds multiple ligands with negative cooperativity, which of the following is true? Each ligand bound increases the dissociation constant for subsequent ligands. Ligands cannot bind to the protein. The dissociation constant is not affected by binding of other ligands. Each ligand bound decreases the dissociation constant for subsequent ligands.
The binding of a ligand quenches the fluorescence of a protein. The following data were acquired: Given that the protein concentration is 0.25 μM, what is the association constant (KA) of the ligand-protein interaction? As this is a rough estimate, you do not need to report uncertainty on your result. The data pic is attached.
12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.
1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value less than 1 b) should exhibit a sigmoidal binding curve c) should show a hyperbolic binding curve d) should give an nH value of 1 e) both a and b f) none of the above
Need help. A protein X binds Ligand Y. The kon characterizing this binding is 1 x 106 M-1s-1, koff is 2 x 10-3 M-1s-1. In your in vitro X-Y binding experiment, at what concentration of Ligand Y half of the Protein X would be bound to Y. Assume that the binding is according to the Lock-and-key model
A protein is allosterically regulated by a molecule. This molecule enhances the binding affinity, and is different from the normal ligand. How would you describe this molecule? A negative homotropic molecule A negative heterotropic molecule A positive heterotropic molecule A positive homotropic molecule
A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.
Calmodulin dependent kinase 1 protein contains 14 tyrosine's 4 tryptophans and 6 phenylalanines the molar extinction coefficient of this protein is approximately 39,200 abs m^-1 cm^-1 not enough information 11,200 abs m^-1 cm^-1 83,200 abs m^-1 cm^-1