Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 8P
Given the following peptide
SEPIMAPVEYPK
a. Estimate the net charge at pH 7 and at pH 12. Assume the pKa values given in Table 5.1
b. How many peptides would result if this peptide were treated with (1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?
c. Suggest a method for separating the peptides produced by chymotrypsin treatment.
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Students have asked these similar questions
A decapeptide was analyzed and the following information obtained. Determine the primary structure of the peptide.
Edman's Degradation: PTH-Ala
Trypsin produces 3 peptides of the following composition:
1. Gly, His
2. Ala, Leu, Lys, Val
3. Arg (2), Phe, Pro
Chymotrypsin produces 2 peptides of the following composition:
1. Ala, Leu, Lys, Phe, Val
2. Arg (2), Gly, His, Pro
Elastase produces 1 amino acids and 3 peptides
1. Ala
2. Leu, Val
3. Arg (2), Lys, Phe, Pro, Gly, His
Arg
Gly
His
Leu
Phe
Pro
Val
4
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser
A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values.
B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly.
C. Would you expect the titration curves of the two peptides to differ? Why or Why not?
Chapter 5 Solutions
Biochemistry: Concepts and Connections
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- A peptide with an amino acid sequence and molecular mass (1028.5193 Da) is given below HVMTLNLGEΚ Determine the maximum number of positive charges of this peptide. а. b. Determine the possible m/z ratio of this peptide at different charge states.arrow_forwardDraw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-Aarrow_forwardH CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14arrow_forward
- For the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues b. What is the charge of the peptide at pH 7.0. Assign the following pKa values: 3,4,6,8,9 c. What is the pI of the peptidearrow_forwardExamine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.arrow_forwardDetermine the pI of the peptide H2N-Ala-Lys-Ser-Arg-COOH at pH 11, please explain why some pKas are used in the solution of the problem while others are not.arrow_forward
- a) Identify and describe the different PEGylation strategies you can use to PEGylate this peptide and draw the chemical structure of the resulting mPEG peptide conjugates. ( draw functional PEGs and corresponding PEGylated products) b) discuss the reaction conditions needed to carry out the PEGylation reactions and explain how pH affects the selectivity of these reactionsarrow_forwardDraw the structure of the PTH derivative you would obtain by Edman degredation of the peptide: ALPF.arrow_forwardConsider a peptide with the sequence Ala-Glu-Arg-Leu. Assume the ionizable groups have the pKa values listed in Table 2.1 of your text. (a) Draw the predominant ionic form of the peptide at pH 7.4. (b) Determine the net charge of the predominant form of the peptide at pH 7.4. (c) Calculate the pI of the peptide.arrow_forward
- peptide Lys-Glu-Trp answer the following questions: Draw the structure of this peptide when all the ionizable groups are fully protonated. How many ionizable groups does this peptide have? Label the pKa for each of the ionizable groups in the structure above. Draw the appropriate titration curve for this peptide on graph paper starting at pH 0 and ending at pH 14. Label the x-axis, y-axis and the pKa Determine the overall net charge of this peptide at each full equivalent point (including 0) where the ionizable group is 100% deprotonated. Determine the pI for this peptide. Determine the average overall net charge of a mixture of this peptide in a solution where pH=8.5.arrow_forward1. Refer to Model 2 for information relevant to this question a) A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? b) What is the pI of Lys-Glu-Ser? 2. Would Lys-Glu-Ser have the same pI as Ser-Glu-Lys? Explain 3. Draw a dipeptide (use R1 and R2 for the side chain R groups) and the resonance tructures of the peptide bond.arrow_forwardGiven the following Peptide: Q6 *H;N-Phe-Asp-Ala-Arg-Gy-His-Arg-Asp-Glu-His-Tyr-CO 6a. What is the peptide's net charge at pH 2.0, pH 6.0, pH 7.4, and pH 10.2? (show work) 6b. What is the approximate isoelectric point of this peptide?arrow_forward
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