1. Draw the structural formula of the amino acid valine that predominates in solution at each of the following pH values. А. рH 3D 7.0 В. рH%3D 12.0 C. pH = 2.0
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- 1.2. Using DEAE-cellulose as ion exchange resin, indicate the starting and ending pH for the narrowest experimental pH range used to separate an amino acid mixture consisting of Cys, His and Leu Starting pH: _____ Ending pH: _____4. A solution containing egg albumin (pl-4.6), B-lactoglobulin (pl-5.2), and chymotrypsinogen (pl=9.5) was loaded onto a column of diethylaminoethyl cellulose (DEAE-cellulose) at pH 5.4.The column was then eluted with a pH 5.4 buffer, with an increasing salt concentration. Predict the elution pattern.A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G 3
- 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 12.5.1. Choose the proper structure of the predominant form of L-M-L-P-D-T at pH 5. Provide a short explanation. 2. Choose the proper structure of the predominant form of L-A-L-Y at pH 11. Provide a short explanation.Given the following information about amino acid tyrosine answer questions 1 & 2: A. O H HO OH HO HO рказ 10.1 H NH₂ CH₂OH A. NH3 С. НО 1. Which of the above forms of tyrosine will be predominant in a solution with pH 9.5? 2. Which of the above forms of tyrosine is a cation? Answers to Questions 3 & 4 should be selected from the following choices: CH₂OH Holl O OH B. NH₂ pka2 9.01 conj acid OH В. НО "OH D. HO HO H OH pka1 2.2 O H -OH CH₂OH C. NH3 HO NH₂ O HO OH D. 3. Which of the monosaccharides above is a non-reducing sugar? 4. Which of the monosaccharides above is an aldotetrose? 5. What is the main functional group in a protein? ||||OH
- 1. Shown below is the chromatogram for some amino acid standards and two unknowns. Each unknown consists of just a single amino acid. Answer the following questions based on this chromatogram. Solvent Frort Ala Ser Asp Are UrkX Unk Y a) Explain the trend in the distances travelled by the standard amino acids. b) Calculate the R¢values of the standard amino acids and the two unknowns. Show your computations. c) Based on your calculations, what are X and Y? d) Are you able to identify X unambiguously? How about Y? e) If you are unable to identify either one of the unknown amino acids, think of a method by which you can separate them from each other. Explain your answer.In ion-exchange chromatography, amino acids are separated on the basis of electro-static interactions and hydrophobic interactions with the resin. The chemical structure of the resin pol-ymer with a negatively charged sulfonic acid group is shown to the right. An elution profile for the aminoacids using this resin is given below. Based on the elution profile above, explain the following:A mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
- Match each charge form of alanine under the pH condition where it would be the predominant form. The pka values for the carboxyl group and amino group of alanine are approximately 2.3 and 9.7, respectively. H H H Н.С — с — соо H Н.С — с — соо Н.С— с —соон Нс — с —соон NH, NH, NH NH, A B D v pH11 2. A Does not occur in significant amounts at any pH 3. D 4. BIn the figures are the titration curves of two amino acids. Consider the first titration. 00 000 pH 10.0 4 14.0 10 9 12.0 3 نیا 8.0 Select the pK, values of each functional group observed on the titration curve. 2 9 6.0 40 20 0.0 0.5 1.0 1.5 2.0 2.5 3.0 equivalents of [CH] Identify which amino acid is being titrated. arginine asparagine histidine lysinea. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain