Based on the Hill Plot below, this protein-ligand interaction displayslogY1-Y52.50-2.5-2.5nH<10log[L]Uncooperative bindingnH>12.5Binding that obeys the Law of Mass ActionNegative cooperativity5

Hill equation developed by Archibald Hill in 1910 quantitatively describing cooperative ligand…

Answered: Based on the Hill Plot below, this…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter32: The Reception And Transmission Of Extracellular Information

Section: Chapter Questions

Problem 11P

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Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.
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.
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.
A binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.
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The Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins would be more easily inhibited by an antagonist? 1.0 Y 0.5 2 A 4 6 B 8 [L] (μM) 10 12 14 16
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
Based on the structure of CBB G-250, explain why it can bind to proteins having basic and hydrophobic amino acid residues.
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.
The following data describe binding of ligand A to a protein, using both Scatchard plots and Hills plots, tell as much as you can about the binding reaction. [A](M) 1X10-6 5 X10-6 1 X10-5 5 x 10-5 1 X 10-4 5 x 10-4 1x 10-3 5X10-3 ṽ 0.101 0.381 0.591 1.116 1.409 1.813 1.899 1.955..
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Draw a fractional binding curve (θ v.s [L]) for a protein binding to one molecule of L with a Kd of 10 mM.

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Based on the Hill Plot below, this protein-ligand interaction displays log Y 1-Y 2.5 0 -2.5 -2.5 Uncooperative binding nH<1 0 log[L] OnH>1 Binding that obeys the Law of Mass Action 2.5 Negative cooperativity 5