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- 6. Draw the structures showing the different protonation states of Arg, and indicate their net charges. Then, compute its pl (isoelectric point).1. Calculate the pH of a 0.05 M solution of HCl. 2. Calculate the pH of a 0.1 M solution of NaOH. 3. Calculate the pH of an acetic acid solution in which [CH3COO - ] = 0.037 M and [CH3COOH] = 0.044 M. (pKa = 4.76) 4. You are conducting a biochemical experiment with an enzyme that has optimal activity at pH = 10.00. You decide to use carbonate (pKa1 = 6.38, pKa2 = 10.30) as the buffer to keep the pH stable throughout the enzymatic reaction. (Recall that the formula for carbonic acid is H2CO3.) You prepare a 0.5 M solution of carbonate buffer at pH = 10.00. Calculate the concentrations of the major carbonate species in your solution. 5. Calculate the pH of the buffer solution in which [H3PO4] = 0.038 M and [H2PO4 - ] = 0.046 M (pKa1 = 2.12, pKa2 = 7.21, pKa3 = 12.32). 6. Add 5.0 mL of 0.1 M NaOH to 80 mL of buffer from question 5 and calculate the pH.13. Calculate the equilibrium constant K'eg, for each of the following reactions at pH 7.0 and 25°C. glucose + Pi a. Glucose 6-phosphate + H20 enz. Glucose 6-phosphatase; AG'O=-13.8kJ/mol
- 3. The chemical equation for the synthesis of ATP is: ADP + Pi +→ ATP + H;:0. AG° = +7.3 kcal/mol. A) Write the chemical equation for the hydrolysis of ATP and note the value of the standard free energy change for this reaction.Table 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
- 1. Draw the structures of the 20 biologically active AA. Under each structure, write the name, one-letter code, and three-letter code followed by the AA classification based on polarity.2) A. What is meant by energetic coupling? What is meant by the term phosphorylation and what role does phosphorylation play in energetic coupling? B. Describe at least one actual example of energetic coupling.For the following tetrapeptide: CKSWa. Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. b. Give the full name of the tetrapeptide. c. Calculate its IpH. d. If the tetrapeptide was subjected to electrophoresis using a buffer solution at pH 7, at which electrode it will migrate?
- 4. Consider the amino acid aspartic acid for this problem. Aspartic acid can be considered a triprotic acid with three ionizable protons with pka's of 1.99, 3.90, and 9.90. When fully protonated aspartic acid has a charge of +1. a. Sketch the titration curve of aspartic acid from pH values of 0.0 to 14.0 below. b. Suppose you began your titration with 10.0 mM aspartic acid. Complete the following concentration table as a function of pH (the first row is "-1" species "-2" species + provided to help you get started): pH 0.0 1.99 2.99 9.90 10.90 "+1" species "0" (neutral species) 0 10.0 mM 0 c. Calculate the isoelectric point of aspartic acid: 0 d. At what pH do you think aspartic acid is least soluble? Explain briefly.2. Mixtures of amino acids can be analyzed by first separating the mixture into its components through ion-exchange chromatography. Amino acids placed on a cation-exchange resin containing sulfonate (-SO₁) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) hydrophobic interactions between amino acid side chains and the strongly hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Asp and Ly, (b) Arg and Met, (c) Glu and Val, (d) Gly and Leu, (e) Ser and Ala3. Consider the following amino acid: HS. OH NH2 a. Draw this structure in a solution of potassium hydroxide. b. Draw this structure in a solution of hydrochloric acid c. Draw this structure as a zwitterion. d. If the pKa of the carboxylic acid group is 2.46 and the pka of the amine group is 9.41, calculate the isoelectric point of this amino acid.