A solution of 0.101 M cysteine is titrated with 0.0253 M HNO3. The pK₁ values for cysteine are 1.70, 8.36, and 10.74, orresponding to the carboxylic acid group, thiol group, and mino group, respectively. Calculate the pH at the quivalence point of the titration. H= + NH₂ HC—CH,—SH FO Cysteine
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- (b) Calculate the pH of 0.0005 mol dm-3 ethanoic acid when its pKa = 4.75 and explain the assumptions made in the calculations CH3COOH(aq) CH3COO-(aq) + H+(aq) Ka = pH =You have 1 M (1 mol/L) solution of amino acid. This amino acid has an alpha carboxyl group with pKa = 2.0 and an alpha- amino group with pKa = 10.0. The pH of the solution is 7.0. Calculate the concentration of the molecular form of this amino acid that has carboxyl group protonated (COOH) and, at the same time, the amino group deprotonated (NH2).An analytical chemist is titrating 50.2 mL of a 0.5100M solution of trimethylamine ((CH3)N) with a 0.7400M solution of HNO3. The pk of trimethylamine is 4.19. Calculate the pH of the base solution after the chemist has added 38.0 mL of the HNO3 solution to it. Note for advanced students: you may assume the final volume equals the initial volume of the solution plus the volume of HNO3 solution added. Round your answer to 2 decimal places. pH = X
- An analytical chemist is titrating 236.4 mL of a 0.3500M solution of trimethylamine ((CH₂)₂N) with a 0.2300M solution of HNO3. The pK₂ of 3 trimethylamine is 4.19. Calculate the pH of the base solution after the chemist has added 77.8 mL of the HNO3 solution to it. Note for advanced students: you may assume the final volume equals the initial volume of the solution plus the volume of HNO3 solution added. Round your answer to 2 decimal places. pH = 0 X ŚA solution of tyrosine is made by dissolving 0.005 mole of tyrosine in 1.0 L of 0.1 M NaOH solution. Draw the structure of the principal chemical form of tyrosine found in this solution at equilibrium given the data below. NH2 pKa (CO2H) = 2.41 pKa (NH2) = 8.67 pka (OH) = 11.01 CHCH2 OH CO2HA solution of 0.138 M aspartic acid, the charge neutral form of the amino acid, is titrated with 0.0460 M NaOH . The p?a values for aspartic acid are 1.990 , 3.900 , and 10.002 , corresponding to the α-carboxylic acid group, the β-carboxylic acid group, and the amino group, respectively. Calculate the pH at the first equivalence point of this titration
- calculate the ph of a 0.465 M solUTION OF ethylamine CH3CH2NH2 and 0.211 M ethylammonium bromide CH3CH2NB3Br. the base dissociation constant kb is 6.31 x 10 -4. what is the pH if 76.0 ml of 0.150 M of a strong acid like HCI is added to 100 ml of buffer solution. what if a strong base like NaOh is added with the same ammount insteadAn analytical chemist is titrating 173.4 mL of a 0.6400 M solution of trimethylamine ((CH,) N with a 0.8100 M solution of HNO3. The p K, of 3 trimethylamine is 4.19. Calculate the pH of the base solution after the chemist has added 59.0 mL of the HNO, solution to it. 3. Note for advanced students: you may assume the final volume equals the initial volume of the solution plus the volume of HNO, solution added. Round your answer to 2 decimal places.Q1. The pKa values of Glutamic acid are 2.2, 4.3 and 9.7. H2N HO. OH (a) Calculate the pH of a glutamic acid solution in which the a-amine group is 80% deprotonated? (show your calculation!) (b) Draw the ionic forms of glutamic acid that exist at the calculated pH.
- a)Calculate the ph of 0.565 M solution of ethylamine, and 0.322 M ethylammonium bromide. The base disassociation constant Kb is 6.31 x 10^-4. b)What is the pH if 107 ml of 0.250 M of a strong acid like HCL is added to 100 ml of the buffer solution? c)What if a strong base, like NaOH is added with the same amount instead?A solution of 0.148 M aspartic acid, the charge neutral form of the amino acid, is titrated with 0.0370 M NaOH. The pK₂ values for aspartic acid are 1.990, 3.900, and 10.002, corresponding to the a-carboxylic acid group, the B- carboxylic acid group, and the amino group, respectively. Calculate the pH at the first equivalence point of this titration. pH = NH3 HC-CH₂-C-OH B a C=O Aspartic AcidYou are conducting a biochemical experiment with an enzyme that has optimal activity at pH = 6.50. 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 0.4 M solution of carbonate buffer at pH = 10.50. Calculate the concentrations of the major carbonate species in your solution. Show your calculations.