16. A quantitative study of the interaction of a protein with its ligand yielded the following results:Ligandconcentration0.51234569.12(μM)v (moles of0.140.310.480.610.680.720.770.790.81ligand boundper mole ofprotein)Plot a graph of ligand concentration versus v. Determine KD, the dissociation constant for theinteraction between the protein and its ligand, from the graph.

I cannot plot the graph as that would be doing your homework.Determine KD:From the graph, read the…

Answered: 16. A quantitative study of 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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1.0 0.9 Z 0.8 15. A pharmaceutical company studied the binding of three different compounds, X, Y, and Z, to a particular protein of interest. For each compound, the fractional saturation (v) was determined as a function of concentration. The results are shown in the figure. Which of the three compounds has the strongest affinity for the protein? Explain. 0.7 X 0.6 > 0.5 0.4 0.3 0.2 0.1 0.0 Y 0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0 2.2 2.4 2.6 2.8 3.0 L(μM)
A peptide with an amino acid sequence and molecular mass (1028.5193 Da) is given below HVMTLNLGEΚ Determine the maximum number of positive charges of this peptide. а. b. Determine the possible m/z ratio of this peptide at different charge states.
When protein X is subjected to dimethylsuberimidate and SDS electrophoresis a 50 kDa band is seen; when the protein X is subjected to SDS electrophoresis without DMS, two bands of 20 kDa and 10 kDa are seen. How many different oligomeric structures of the native protein X are possible, being consistent with these observed results? one two three none of the above which is the answrr? and explain
In a TPN bag contains: Kcal of 1000 ml of D50 W, 1000 ml of 7% amino acids, and 650 ml of 20% lipids. A. How many total kcal is provided by this bag of TPN?
B) An aqueous solution (pH ~7) containing mixture of three amino acids; glycine (G), arginine (R) and glutamic acid (E), was dropped onto center of a solid matrix (e.g chromatographic paper) which is incorporated in an electrical circuit (a). After applying electrostatic potential, the aminoacids are separated as shown in b. Determine amino acids that are labeled as 1, 2 and 3. a) DC Power Supply (OFF) b) DC Power Supply (ON) Solid matrix Solid matrix Cathode Anode Cathode Anode buffer buffer buffer buffer Sample containing amino acids G, R, E
In the Bradford protein determination, the color of a dye changes from brown to blue when it binds to a protein. The intensity of blue color (measured by absorbance of light at a wavelength of 595nm) is proportional to protein concentration. Protein (ug) Absorbance at 595nm 0.00 0.466 9.36 0.676 18.72 0.883 28.08 1.086 37.44 1.280 Use Excel to determine the equation of the line in the format of y = mx + b. (I tried y=0.0218x+0.4706 and it was wrong) Using the calibration curve for the Bradford protein determination in the previous question, determine the number of micrograms of protein in an unknown if it gave an absorbance of 0.973. I tried 23.505 and it was wrong
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
17 Peptides can be separated using an ion-exchange column based on their isoelectric (pl) values. At which pH values would two different peptides, one with a pl of 5.6 and the other with a pl of 8.9, bind to a cation- and anion-exchange column? Each peptide may be capable of binding to each column at more than one pH value. anion-exchange column at pH = 3.5 cation-exchange column at Answer Bank pH = 3.5 peptide A pf = 5.6 peptide A peptide B pl = 89 pl= 5.6 peptide B pl = 8,9 pH= 7.4 pH = 7,4 peptide A pl= 5.6 peptide A pl= 5.6 pH = 10.1 pH = 10.1 peptide B V oppdad pl=56 pl= 89
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
Two proteins, A and B, bind to the same ligand, L, with the binding curvesshown below. What is the dissociation constant, Kd , for each protein? Which protein (A or B) has a greater affinity for ligand L?
1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?
Please draw a visual representation

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