A protein binds a ligand with a ka value of 7.4 x 104 M-1s-1 and a kd value of 6.4 x 10-4 s-1. What is the KD value of this binding event in units of nM? Please report your answer to two significant figures and include units.
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A protein binds a ligand with a ka value of 7.4 x 104 M-1s-1 and a kd value of 6.4 x 10-4 s-1. What is the KD value of this binding event in units of nM? Please report your answer to two significant figures and include units.
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- 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 nM1) Protein A has a binding site for ligand X with a dissociation equilibrium constant of 4.0 x 10-8 The association equilibrium constant for ligand X and protein A is: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
- An enzyme binding equilibrilum has a Kd = 50 mM. What concentration of ligand (in mM) is required in order to bind 10% of the enzyme?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.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 fractional occupancy of a protein binding site when the ligand concentration (L) = 1mM and the ligand equilibrium binding constant at the binding site K10 = 10microM. A. 0.01 B.0.1 C.0.91 D.0.99 E. none of the listed valuesA protein binds a ligand with a KD value of 0.25 M. If you are at a ligand concentration of 0.63 M, what is the fraction bound? Please report your answer to two significant figures. There should be no units in your answerWe have a mixture of 100 mL of Fe3+ solution (1.00 × 10–3 M) and 100 mL of A- ion solution (1.00 × 10–3 M). The mixture has a deep blue color, indicating the formation of a complex between Fe3+ and A-. From spectrophotometric analysis, we find that 30.0% of the Fe3+ is in the form of a complex, where there are two probable formulae: FeX2+ or FeX3. a. Balance the following equations and calculate the concentrations of the remaining species. b. After reaching equilibrium states, write the equilibrium expressions and the equilibrium constants for both cases in (a).
- If the association constant, Ka, for a certain protein-ligand pair is 50,000, what is the dissociation constant, Kd? Please provide your answer in decimal form, not scientific notation.The red color of soil is often due to the presence of iron. Metal ions are extracted from soil by stirring the soil in acid and then filtering the solution. One method for the analysis of Fe2+ is to form the highly colored Fe2+–thioglycolic acid complex. The complex absorbs strongly at 535 nm. Calibration standards of 1.00, 2.00, 3.00, 4.00, and 5.00 ppm are prepared by transferring appropriate amounts of a 10.0 ppm working solution of Fe2+ into separate 50-mL volumetric flasks, each of which contains 5 mL of thioglycolic acid, 2 mL of 20% w/v ammonium citrate, and 5 mL of 0.22 M NH3. After diluting to volume and mixing, the absorbances of the standards are measured. a)Use the data table below to prepare a calibration curve (absorbance versus concentration in ppm). Fit the data to straight line and find the equation for the straight line and the R2 value. (Hint: Think about what to do with the absorbance of the blank.)The red color of soil is often due to the presence of iron. Metal ions are extracted from soil by stirring the soil in acid and then filtering the solution. One method for the analysis of Fe2+ is to form the highly colored Fe2+–thioglycolic acid complex. The complex absorbs strongly at 535 nm. Calibration standards of 1.00, 2.00, 3.00, 4.00, and 5.00 ppm are prepared by transferring appropriate amounts of a 10.0 ppm working solution of Fe2+ into separate 50-mL volumetric flasks, each of which contains 5 mL of thioglycolic acid, 2 mL of 20% w/v ammonium citrate, and 5 mL of 0.22 M NH3. After diluting to volume and mixing, the absorbances of the standards are measured. a)What is the effect on the reported concentration of iron in the sample if there is a trace impurity of Fe2+in the ammonium citrate?