Does the titrated amino acids appear to be acidic, basic, or neutral amino acids? Please explain your conclusion with reference to the data and to theory.
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Does the titrated amino acids appear to be acidic, basic, or neutral amino acids? Please explain your conclusion with reference to the data and to theory.
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- Draw the titration curve for serine and glutamic acid, starting at pH1, going to 14 andadding equivalents of base1) You are asked to prepare a buffer for a protein assay. This protein works best at a slightly acidic pH of 5.5. a. From the list of Acids and conjugate bases which pair would you pick. (The list is in the attached image) b. You are asked to make a 1M stock solu on of the Buffer, how many grams of each acid and base would you need to make a 500mL stock. c. For the experiment, the final concentra on of the buffer should be 50mM. How many mL of your stock would you need to make 2L. Hint: M1V1=M2V2Sketch a titration curve for the amino acid cysteine, and indicate the pKa vaules for all titratable groups.
- Tyrosine is a triprotic weak acid, with pKa1=2.41, pKa2=8.67, and pKa3=11.01. a) calculate the final [OH-] of a solution that starts with .30M of the fully basic form. Do not assume the concentration of base is constant. b) at what pH range(s) would tyrosine act best as a buffer? c) calculate the pH of a solution at equilibrium which started with 0.043M at the monoprotonated H2A- form *Please show all work and not just answers, I'm looking to understand how to solve problems like these! TIAGive typed full explanation not a single word hand written otherwise leave it Calculate the isoelectric point of the amino acid histidine by plotting the titration curve. (pka values α-COOH=1.82, α-NH2= 9.17, imidazole= 6.0)What is the equivalence point pH of a 0.1M solution of phenylalanine that is fully titrated with NaOH?
- What is the molarity of the FAS titrant solution given the following:Vol of K2Cr2O7: 100 mLVol of FAS titrant: 15.2 mLMolar mass of FAS: 284.1 g/molMass of FAS: 24.135 gSketch the titration curve of CRIP and draw the corresponding predominant structue at each equivalence point. Determine: 1) PI 2) Charge of the peptide above at pH 10 3) Charge of the peptide above at pH 24) Charge of the peptide above at around 12.5?30ml of 0.06M solution of protonated form of anion amino acid methionine (H2A+) is treated with0.09M NaOH.calculate pH after addition of 20 ml of base.pKa1=2.28 and pKa=9.2 please answer this question .with explanation
- 1.What is the most effective pH buffering range for a alazarin yellow indicator? (benzoic acid Ka = 7.9 × 10-12) A. Cannot be determined. B. 5.3 – 7.3 C. 4.7 – 6.7 D. 8.8 – 10.8 E. 10.1 - 12.1 2. What is the dominant form of aspartic acid (a triprotic acid) at a pH of 1.50 (pKa1 = 1.990, pKa2 = 3.900, pKa3 = 10.002)? A. H3A and H2A- are equal B. H2A- C. HA2- D. H3A 3. Determine pCl and pAg if 20 mL of a 0.1 M AgNO3 solution is titrated with 6 mL of 0.2 M HCl. pKsp(AgCl) = 9.8. A. pAg = pCl = 4.9 B. pAg = 8.29 and pCl = 1.5 C. pAg = 9.8 and pCl is undetermined. D. None of the above.Calculate the pH: - 0.20 M arginine hydrochloride - 50.0 mLs of 0.10 M arginine hydrochloride to which 50.0 mLs of 0.10 M NaOH have been added.Please sketch the titration curve of lysine. Then annotate X-axis, Y-axis, each pKa, PI and ionizable forms of lysine on the curve. Note: the value of pKa or PI is not required.