they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning.

they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning.

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 50AP: The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in...

See similar textbooks

Similar questions

1.Give the general association equilibrium expression and the association equilibrium constant (Ks) for the reversible binding of a protein (P) to a ligand (L).
Ligand L binds to a binding protein with a Kd of 400 nM. Calculate the ligand concentration based on the fraction of binding sites occupied by the ligand (Y). Calculate the ligand concentration when Y is 0.25. Calculate the ligand concentration when Y is 0.60. Calculate the ligand concentration when Y is 0.95. [L] : = [L] = [L] = μM μM μM
For the binding graph of Protein B with ligand X on the right, (i) Estimate the K, for Protein B with ligand X. Explain how you determined the Ka. (ii) Protein B binds to ligand Z with a Ka = 4.8 x 106. Display a curve on the graph to represent Protein B binding to ligand Z. Using the information you have, explain which ligand Protein B has higher affinity for. 0.8 0.6 0.4 0.2 0 1 2 3 4 5 6 7 8 9 10 [Ligand] umol L An uncatalyzed reaction has AG = 59.5 kJ mol and a rate of reaction that is 6.31 x 109 umol s1 at 25.0 °C and pH 8.1. When an enzyme is added, the rate of reaction is 1.49 umol s' at 25.0 °C and pH 8.1. Calculate the activation energy of the catalyzed reaction.
1. From the following binding data of a ligand binding to a protein, which set of the K50 and Hill Coefficient is the most likely? [Ligand](M) 0.1 Y 0.2 0.2 0.5 0.4 0.8 0.6 0.9 0.2 M, 1 0.04 M, 2 0.008 M, 3 0.45 M, 0.5
You prepare a solution of protein and its ligand where the initial concentrations are [Protein] = 10 nM and [Ligand] = 10 nM. At equilibrium you measure the [PL] = 5 nM. If the protein - ligand association can be represented by: P + L <--> PL What is the dissociation constant (Kd) of the protein for the ligand under the solvent conditions you have chosen? a. 1 nM b. 0.2 nM-1 c. 5 nM d. 10 nM
Protein X binds to Ligand W with a dissociation constant of .15 μmol. what is the concentration of W 75% of the protein is free (ie, unbound)?"
You perform a ligand binding assay using a newly isolated protein with its natural ligand and plot the resulting data. 1.0 Use the graph of bound ligand fraction (Y) versus ligand concentration ([ligand) to estimate the dissociation constant (Ka) and the association constant (K,). 0.75 > 0.5 0.25 0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 (ligand) (M) 0.10 Ka = K. - 10 M- incorrect Incorrect
19. The association constant of protein X for ligand Y is: 100 micromolar. At what concentration of ligand is half fo the protein bound?
From the Hill Plot below, the KD of the first binding event for the receptor-ligand system under study is: 10 8 6 4 2 0 -2 4 6 8 10 (0=1) 601 log -4- -6 -6 -4 -2 0 2
what is the Ligand receptor interaction prediction of the structure in the picture that i attached thank you
The protein Westlin is 64% occupied when the concentration of its ligand, iocane, is 5 uM. Given this, the Kp of Westlin for iocane is uM. If the total concentration of Westlin is 2 nM, and the concentration of iocane is 10 uM, you know that the concentration of free protein must be nM.
Two different proteins X and Y are dissolved in aqueous solution at 337.0 C. The proteins bind in a 1:1 ratio to form XY. A solution that is initially 1.460 mM in each protein is allowed to reach equilibrium. At equilibrium, 0.250 mM of free X and 0.250 mM of free Y remain. What is Kc for the reaction? 4.69e+04 The answer is not shown. 1.94e+04 2.63e+04 2.47e+04