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- 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?For the amino acid arginine: Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. Provide labels (A, B, C, etc.) for each form. b. Calculate the IpH of the amino acid. c. At what pH range(s) it can act as a buffer? d. What will be the predominant form(s) of the amino acid at pH (i) 1.5; (ii) 3.0; (iii) 4.5; (iv) 6.0; (v) 7.5 and (vi) 9.0?The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. 2 1.5 1 0.5 -0.5 -1 4 6. 8 10 12 14 pH a. Which of the following triprotic amino acids is this? [ Select ] b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pka values in the pKa table for amino acids, which was in video one of today's lecture) [ Select ] c. What form of this amino acid dominates at a pH of 8? Please select the correct form for each ionizable group. Alpha amino [ Select ] Alpha carboxyl [ Select ] R [ Select ] Net Charge
- The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. Net Charge 0 2 4 Alpha amino [Select] 6 R [Select] pH a. Which of the following triprotic amino acids is this? Alpha carboxyl [Select] 8 10 12 [ Select] 14 1 0.5 0 -0.5 -1 b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pKa values in the pKa table for amino acids, which was in video one of today's lecture) [Select] -1.5 c. What form of this amino acid dominates at a pH of 14? Please select the correct form for each ionizable group. -2The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. 2 1.5 1 0.5 -0.5 -1 4 8 10 12 14 pH a. Which of the following triprotic amino acids is this? Histidine b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pka values in the pKa table for amino acids, which was in video one of today's lecture) 7-8 c. What form of this amino acid dominates at a pH of 8? Please select the correct form for each jonizable group. Alpha amino NH3+ Alpha carboxyl СОО- R| NH Net ChargeYou are super jazzed because your protein is purified and at a concentration of 600 μg in 1.75 ml of buffer. Convert this concentration to mM. Note that biochemisfunase has a molecular weight of 54,321 Daltons (which is just another unit for g/mol). Show your calculations.
- You have prepared a BSA serial dilution (ug ml) to construct a protein standard curve, for which the equation is: Y=0.007X + 0.02. Use this equation to determine the starting concentration of 3 separate protein samples: a. 1:10 dilution with absorbance 0.3 nm b. 1:10 dilution with absorbance 0.2 nm c. 1:50 dilution with absorbance 0.1 nm. Please use a separate lme for each answer, preceded by the corresponding letter. Don't forget units on each answer. For the toolbar, press ALT+F10 (PC) or ALT+FN+F10 (Mac).Use the table below to answer the question being asked: Protein Ovalbumin Insulin Fibrinogen y-globulin Collagen Hemoglobin (monomer) Myoglobin Isoelectric pH 4.6 5.4 5.8 6.6 6.6 7.1 7.0 Molecular weight (KDA) 45 5.7 340 160 115 16 16.7 A. Given the 7 proteins in the table, will they all be separated properly using Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE)? Why or why not? Kindly justify your answer. B. Manually sketch the appearance after visualization of a protein mixture containing the 7 proteins in the table when subjected to Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE).Use the table below to answer the question being asked: Protein Ovalbumin Insulin Fibrinogen y-globulin Collagen Hemoglobin (monomer) Myoglobin Isoelectric pH 4.6 5.4 5.8 6.6 6.6 7.1 7.0 Molecular weight (KDA) 45 5.7 340 160 115 16 16.7 A. Given the 7 proteins in the table, will they all be separated properly using two-dimensional (2D) gel electrophoresis? Why or why not? Kindly justify your answer. B. Manually sketch the appearance after visualization of a protein mixture containing the 7 proteins in the table when subjected to two-dimensional (2D) gel electrophoresis.
- The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.A protein gives, under conditions of buffer composition, pH, and temperature that are close to physiological conditions, a molecular weight by sedimentation equilibrium measurements of 140,000 g/mol. When the same protein is studied by SDS gel electrophoresis in the absence or presence of the reducing agent β-mercaptoethanol (BME), the patterns seen in lanes A and B respectively are observed. Lane C contains standards of molecular weight indicated. From these data, describe the native protein, in terms of the kinds of subunits present, the stoichiometry of subunits (that is, how many of each subunits are present), and the kinds of bonding (covalent, non-covalent) existing between subunitsConsider the following situation; Fresh pineapple contains the enzyme bromelain that hydrolyzes peptide bonds in proteins. a. The directions in making a gelatin (protein) dessert say not to add fresh pineapple. However, canned pineapple where pineapple is heated to high temperatures can be added. Why? b. Fresh pineapple is used in a marinade to tenderize tough meat. Why? c. What structural level of a protein does the bromelain enzyme destroy?