Given the curves below, what are the dissociation constants for proteins A and B?(%) Supurg10080-60402002030Concentration (nM)10A=28, B=3A=3, B=28Cannot determine Kp from this plotA=10, B=2BA=2, B=10A40 Based on the plot provided below, which of the following statements is incorrect?Binding (%)1008040201020 30Concentration (nM)bBAA binds the ligand tighter than B40B binds the ligand tighter than Ab and cThe Kp of A> the Kp of B

Kd is dissociation constant which is equal to ligand concentration at half maximum saturation of…

Answered: Given the curves below, what are the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
Number 3
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Describe how you would make the following solution containing two enzymes. 1 mL total volume in Buffer X with 10nM of enzyme A and 50nM of enzyme B You are given a solution of enzyme A at 1 mg/mL and a solution of enzyme B at 1 mg/mL. The molecular weight of enzyme A is 75,000 g/mol and the molecular weight of enzyme B is 130,000 g/mol.
3. Compute for the amount of each component of KCN broth if you were to prepare 280 ml. Express your answers using two decimal places. Follow this format in typing your answers: answerabbreviated unit (e.g. 3.00 g, 0.75 ml, 10.25 mg): Components Amount per liter Polypeptone 3.0 g NazHPO4 5.64 g (Available as NazHPO4 · 7H2O*) Monopotassium phosphate 0.225 g Sodium chloride 0.5% KCN 0.075 g (Available as 10,000 ppm solution) *MW (g/mol): Na-23; P-31; H-1; 0-16 3.2. Na2HPO4 • 7H2O!'
Fill up the two missing values inside the two circles knowing that the total reaction volume is 2mL. 1) Dilution fraction 2) Water Don't include units in your answer. Membrane Brillant blueR 1g/L Dilution Sample suspension fraction (μL) (μL) 1) Control ? 0 50 2) 1/200 ? 10 50 3) 1/100 0.01 20 50 4) 1/50 ? 40 50 5) 1/20 100 50 Phosphate pH11, 0.2M (ml) 1 1 1 1 1 Water (mL) 0.95 ? ? ?
1.You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its AGO for unfolding is 1.2 kcal/mol at 37° (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 10-fold dilution of your pure protein in solution (by this, we mean that 100 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
The units for the unimolecular reversible rate constant for the forward reaction are ○ M sec-1 sec M-1 sec-1 sec-1
For the following reaction X + YA + B at 300 K, it is found equilibrium constant equal to 10. Therefore, AG & AGⓇ of the reaction at 300 K respectively are - Answer b
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
You run 5 standard proteins listed below on a size-exclusion (gel filtration) column with limit of 200,000Da. Please draw a chromatogram on a separate page with each peak and both axes labeled. Protein B-Amylase Alcohol dehydrogenase Bovine albumin Carbonic anhydrase Cytochome A280 MW 223,800 0.5 82,000 0.6 66,463 0.45 30,000 0.43 12,000 0.8
Consider the proteins in the table below. Protein Isoelectric point (pl) М.W. Alcohol dehydrogenase 150,000 5.5 Cytochrome C 12,400 10.5 Serum albumin 66,000 5.3 B-Amylase 200,000 5.7 Apoferitin 443,000 4.0 Fill in the blank. If the mixture of proteins above was subjected to anion exchange chromatography at pH 8, from the column. would be the first protein to elute

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Given the curves below, what are the dissociation constants for proteins A and B? 100 80- 60 40 20 0 0 10 20 30 Concentration (M) A=28, B=3 A=3, B=28 Cannot determine Kp from this plot O A=10, B=2 B A=2, B=10 A 40