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- 1. Consider the peptide with amino acid sequence NICE. a. Write the full name and the three-letter abbreviations of the amino acids in the реptide. b. Calculate the net charge of the peptide at pH 7.0. Show you work in a table. с. Calculate the pI of the peptide. Show you work in a table.4. A. Draw the structure of the following peptide sequence at pH 2.0: ASP-ALA-THR-LYS-GLY B. What is the net charge of this pentapeptide at pH 2.0?1. Consider the peptides P-A-I-G-E and M-A-T-T. a. Draw the structure of each peptide at a pH of 7.0 b. Draw the structure of each peptide at a pH of 12.0 c. Calculate the pl of both peptides. Based on your answer, do you think these two peptides can be separated using ion exchange chromatography at a pH of 5? Explain.
- 1. Draw an approximate titration curve of the following amino acid. Label the approximate isoelectric point of arginine on the curve and be sure to label the axis of the graph appropriately. You DO NOT need to draw the structure of this amino acid here. Pk1= 1.92, pk2=8.99 and pk3=12.48. Show your work for determining the isoelectric point. You can draw out your curve within the text box or upload a drawing. A▾ B I - I B 74. Write the structure of each of the following peptides at pH 7: a. Alanylphenylalanine b. Threonylcysteine c. Phenylalanyltryrosylleucine d. Glycylvalylserine 5. Tripeptides are composed of three amino acids linked by peptide bonds. Given a set of amino acids, you can make several different tripeptides. a. Use the three-letter shorthand notations to name all the tripeptides that can be made from serine, tyrosine, and glycine. Each amino acid will be used once in each tripeptide. b. Draw the complete structure of the tripeptides that have glycine as the N-terminal amino acid.4. a. Give the full names of the amino acids in this peptide. НзN — CH—С-N—CH— С-N—CH—С—О ČH3 H ČH,OH H. CH2 -ОН b. Calculate the isoelectric point (pl) of a peptide with sequence SNARE. Show your work in a table, giving the pKa values of the ionizable groups, pH, and charges. Step marks are counted. Don't need to write “protonated" or “deprotonated".
- 2. Complete the following for serine, tyrosine, and gylcine. a. Draw the amino acid. b. Circle the side chain. c. Identify whether it is polar, nonpolar, acidic, or basic. d. Look for the pK₁, pk2, and PKR (if there an ionizable side chain) e. At what pH will it exist as a zwitterion? f. What is the range of pH values when it will be positively charged? g. What is the range of pH values when it will be negatively charged?1. Consider the peptide with amino acid sequence NICE. а. Write the full name and the three-letter abbreviations of the amino acids in the peptide. b. Calculate the net charge of the peptide at pH 7.0. Show you work in a table. Step marks are counted. с. Calculate the pI of the peptide. Show you work in a table. Step marks are counted.7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thr a. Write out the single letter sequence of this peptide. b. What is the overall charge of the peptide? Is it acidic? Basic? c. Draw the chemical structure of the peptide at pH 7.0 and show any charged groups d. What is the classification of each amino acid in this peptide regarding polarity and charge? 8. The following proteins represent a wide range of molecular weights and isoelectricpoints. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at phH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated…
- 5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=01. Draw the structural formula of the amino acid serine that predominates in solution at each of the following pH values. A. pH = 4.0 В. рH %3D9.0 С. рH %3D 7.0 %3D6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…