Question

Problem 1. (25 points) You study ligand binding to two proteins, A and B. You measured the concentration, [PL], of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound-protein concentration. Protein A [L], µM | [PL], µM 0 | 0.000 5 | 0.040 10 | 0.067 50 | 0.143 200 | 0.182 500 | 0.192 2000 | 0.198 Protein B [L], µM | [PL], µM 0 | 0.00 15 | 0.21 30 | 0.33 100 | 0.55 300 | 0.68 1000 | 0.74 3000 | 0.76 Based on these data, answer the following questions: (1) Determine the Kd values for each of the proteins. Explain your assumptions. Since adding more ligand did not change [PL], we can assume that a full saturation has been reached, therefore [Ptotal] = [PL] at the end of the titration. A: 20 µM; B: 40 µM

          Problem 1. (25 points) You study ligand binding to two proteins, A and B. You measured the concentration, [PL], of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound-protein concentration.

Protein A
[L], µM | [PL], µM
0 | 0.000
5 | 0.040
10 | 0.067
50 | 0.143
200 | 0.182
500 | 0.192
2000 | 0.198

Protein B
[L], µM | [PL], µM
0 | 0.00
15 | 0.21
30 | 0.33
100 | 0.55
300 | 0.68
1000 | 0.74
3000 | 0.76

Based on these data, answer the following questions:
(1) Determine the Kd values for each of the proteins. Explain your assumptions.

Since adding more ligand did not change [PL], we can assume that a full saturation has been reached, therefore [Ptotal] = [PL] at the end of the titration.
A: 20 µM; B: 40 µM

Show more…

Problem 1. (25 points) You study ligand binding to two proteins, A and B. You measured the concentration, [PL], of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound-protein concentration.

Protein A
[L], µM | [PL], µM
0 | 0.000
5 | 0.040
10 | 0.067
50 | 0.143
200 | 0.182
500 | 0.192
2000 | 0.198

Protein B
[L], µM | [PL], µM
0 | 0.00
15 | 0.21
30 | 0.33
100 | 0.55
300 | 0.68
1000 | 0.74
3000 | 0.76

Based on these data, answer the following questions:
(1) Determine the Kd values for each of the proteins. Explain your assumptions.

Since adding more ligand did not change [PL], we can assume that a full saturation has been reached, therefore [Ptotal] = [PL] at the end of the titration.
A: 20 µM; B: 40 µM

Added by Randy R.

Chemistry: Structure and Properties

Nivaldo Tro 2nd Edition

Instant Answer

Solved by Expert Shyam P

04/21/2022

Step 1

Kd, or the dissociation constant, is a measure of the affinity of a ligand for a protein. It is the concentration of ligand at which half of the protein is bound to the ligand. A lower Kd indicates a higher affinity of the protein for the ligand. To calculate Kd, Show more…

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Problem 1. (25 points) You study ligand binding to two proteins, A and B. You measured the concentration, [PL], of the ligand-bound form of the protein at various ligand concentrations, [L]. The data are summarized in the two tables below. Note that you do not know the total concentration of the protein, but you know that adding more ligand did not noticeably change the bound-protein concentration. Protein A [L], µM | [PL], µM 0 | 0.000 5 | 0.040 10 | 0.067 50 | 0.143 200 | 0.182 500 | 0.192 2000 | 0.198 Protein B [L], µM | [PL], µM 0 | 0.00 15 | 0.21 30 | 0.33 100 | 0.55 300 | 0.68 1000 | 0.74 3000 | 0.76 Based on these data, answer the following questions: (1) Determine the Kd values for each of the proteins. Explain your assumptions. Since adding more ligand did not change [PL], we can assume that a full saturation has been reached, therefore [Ptotal] = [PL] at the end of the titration. A: 20 µM; B: 40 µM

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Transcript

0:00 Hello.

00:01 So in this question, we are studying about the ligand binding to two proteins.

00:16 And we are given some information that is a table it is given here.

00:21 So we can see that from the table that it is seen that adding more ligand did not change the concentration.

00:30 So for which we can assume that the full saturation, that is a saturation, full saturation was reased.

00:43 So it shows that p total is equal to pl at the end of the, at the end of titration.

00:58 So for protein a, for protein a, this kd is equal to 20 mu m.

01:09 And for protein b, for protein b, this kd, that is a dissociation constant, it is equal to 40 mu m.

01:29 Now, we know that if the dissociation constant value, if it is low, then it has the high affinity.

01:39 Low dissociation value shows that low or we can say there is a less dissociation can be occurred.

01:50 Therefore, that is the high affinity between the molecules which shows that the bond is, bond tightening is very high.

02:03 Or we can say that it is the bond between the molecules or the atom, it is very strong.

02:12 If the value of this dissociation constant is high, then easily it may dissociate into its ion.

02:21 That means there is a low affinity and therefore we can say bond tightening it is very low between the molecules...

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