a)The equilibrium reaction for the aqueous dissociation of acetic acid is shown below.CH3COOH(aq) = CH3COO-(aq) + H+ (aq)Given the data in the table below and your knowledge of the "chemical standardstate" (X) and the “biochemical standard state” (Xº'), answer parts a) to e).c)For the dissociation of acetic acid at 298.15 K,calculate AG and the corresponding pK₁.b) Even though by definition, AfG©(H+ (aq)) = 0and_AƒGº¹(H+(aq)) = 0, these are differentphysical quantities. What precisely does eachrepresent?Calculate at 298.15 K, AG' for CH3COOH(aq)and CH3COO¯(aq).Gibbs free energy of formation,in units of kJ mol-¹, at T = 298.15 KAfGeA¢G°-396.5-369.30CH3COOH(aq)CH3COO- (aq)H+ (aq)d) For the dissociation of acetic acid at 298.15 K, calculate ArGº¹.LOXF0Finally, using the formula to convert between standard states, show that thatyour calculated values of AG and A.Gº are in agreement.jonlythis

Chemical standard state is defined by standard conditions in chemical systems. These standard…

Answered: Finally, using the formula to convert…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter3: The Plasma Membrane And Membrane Potential

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Problem 1SQE: Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following...

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Given the titration curve of the hypothetical polyprotic acid X at 0.100 M concentration (pKa1=4.0, pKa2=8.0, pKa3=12.0) titrated with 0.600 M NaOH, identify the pH at point C, H, E, and M.
To characterize a purified enzyme, a biochemist has determined the reaction initial velocities, at various [S]。, using three different conditions: a) In the presence of the enzyme alone. b) In the presence of the enzyme and of a non-metabolizable substrate analog (compound A, at 150 µm). c) In the presence of the enzyme and of a compound that binds to the enzyme at a site different from that of the substrate (compound B at 60 µM). From his experimental results, he has drawn the Lineweaver-Burk plots (below). 1- Indicate which symbols (circles, triangles, diamonds) on the graph correspond to the experiments a, b, c. Justify your answer. 2- Determine graphically Km, Kmapp., Vmax and Vmaxapp. 3- Determine the inhibition constants Ki for the compounds A and B (i.e. the dissociation constants of complexes El). 1/V₁ (min.xM-¹) -6000 -4000 -2000 2.5 2 1.5 1 0.5 0 2000 4000 1/[S], (M-¹) 6000
Sketch a titration curve and the structures of the major ionic forms of glutamic acid that exist in solution at the noted parts of the titration curve. Refer to the fully pronated glutamic acid and the pKa.
The absorption of ketoconazole has been shown to be impaired in patients with drug-induced achlorhydria. The drug absorption was increased significantly to approximately 65% when the drug was taken with an acidic beverage such as Coca-Cola (pH 2.5). Ketoconazole is a synthetic azole antifungal agent and a weakly dibasic compound with pKa of 2.9 and 6.5. Using the information provided and the pH partition hypothesis, justify the use of Coca-Cola to improve the absorption of this antifungal agent.
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?
A monoprotic weak acid, HA, dissociates in water according to the reaction HA(aq) = H+ (aq) + A¯(aq) The equilibrium concentrations of the reactants and products are [HA] = 0.220 M, [H+] = 3.00 × 10−4 M, and [A¯] = 3.00 × 10−4 M. Calculate the value of pKa for the acid HA. pKa =
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.

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