FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
5th Edition
ISBN: 9781119498742
Author: Voet
Publisher: WILEY
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Chapter 5, Problem 34CQ
Summary Introduction
To determine: The sequence of the intact peptide.
Concept introduction: Proteins are made up of one or more amino acids linked together to form a chain. The building blocks of the protein is called amino acid. Amino acids are termed as residues if they release a hydrogen ion from the
Given:
- Cleavage with chymotrypsin yields three peptides: Leu-His-Lys-Gln-Ala-Asn-Gln-Ser-Gly-Gly-Gly-Pro-Ser, Gln-Gln-Ala-Gln-His-Leu-Arg-Ala-Cys-Gln-Gln-Trp, Arg-Ile-Pro-Lys-Cys-Arg-Lys-Phe.
- Cleavage with trypsin yields seven smaller peptides: Arg, Ala-Cys-Gln-Gln-Trp-Leu-His-Lys, Cys-Arg, Gln-Ala-Asn-Gln-Ser-Gly-Gly-Gly-Pro-Ser, Phe-Gln-Gln-Ala-Gln-His-Leu-Arg, Ile-Pro-Lys, and Lys.
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Chapter 5 Solutions
FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
Ch. 5 - Prob. 1ECh. 5 - Prob. 2ECh. 5 - 3. Which peptide has greater absorbance at 280...Ch. 5 - 4. Protein X has an absorptivity of 0.4 mL · mg?1...Ch. 5 - 5. You are using ammonium sulfate to purify...Ch. 5 - Prob. 6ECh. 5 - 7. (a) In what order would the amino acids Arg,...Ch. 5 - Prob. 8ECh. 5 - 9. Explain why a certain protein has an apparent...Ch. 5 - 10. Determine the subunit composition of a protein...
Ch. 5 - 11. Explain why a protein, which has a...Ch. 5 - 12. A protein has an apparent mass of 800 kD by...Ch. 5 - 13. Explain why the dansyl chloride treatment of a...Ch. 5 - 14. Identify the tint residue obtained by Edman...Ch. 5 - 15. A pentapeptide has the sequence NNKNN (using...Ch. 5 - 16. The peptide in Problem 15 was sequenced by...Ch. 5 - 17. In site-directed mutagenesis experiments, Gly...Ch. 5 - 18. Below is a list of the first 10 residues of...Ch. 5 - Prob. 19ECh. 5 - Prob. 20ECh. 5 - Prob. 21CQCh. 5 - Prob. 22CQCh. 5 - 23. What fractionation procedure could be used to...Ch. 5 - Prob. 24CQCh. 5 - 25. Purification tables are often used to keep...Ch. 5 - Prob. 26CQCh. 5 - 27. You must cleave the following peptide into...Ch. 5 - 28. You wish to determine the sequence of a...Ch. 5 - Prob. 29CQCh. 5 - Prob. 30CQCh. 5 - 31. You wish to determine the sequence of a short...Ch. 5 - Prob. 32CQCh. 5 - Prob. 33CQCh. 5 - 34. You wish to sequence the light chain of a...Ch. 5 - Prob. 1MTE
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- Problem 15 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 4 of 15 4G 54% Done On the following Lineweaver-Burk -1 plot, identify the by dragging the Km point to the appropriate value. 1/V 40 35- 30- 25 20 15 10- T Км -15 10 -5 0 5 ||| 10 15 №20 25 25 30 1/[S] Г powered by desmosarrow_forward1:30 5G 47% Problem 10 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a competitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' s mM¹ with 10 mg pe 20 V' 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
- Problem 14 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:36 CO Problem 9 of 15 4G. 53% Submit Using the following reaction data points, construct a Lineweaver-Burk plot by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Based on the plot, determine the value of the catalytic efficiency (specificity constant) given that the enzyme concentration in this experiment is 5.0 μ.Μ. 1 [S] ¨‚ μM-1 1 V sμM-1 100.0 0.100 75.0 0.080 50.0 0.060 15.0 0.030 10.0 0.025 5.0 0.020 Answer: ||| O Гarrow_forwardProblem 11 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a noncompetitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' 20 V' s mM¹ with 10 μg per 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
- Problem 13 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 8 of 15 4G. 53% Submit Using the following reaction data points, construct a Lineweaver-Burk plot by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Based on the plot, determine the value of kcat given that the enzyme concentration in this experiment is 5.0 μM. 1 [S] , мм -1 1 V₁ s μM 1 100.0 0.100 75.0 0.080 50.0 0.060 15.0 0.030 10.0 0.025 5.0 0.020 Answer: ||| Гarrow_forward1:33 5G. 46% Problem 12 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without an uncompetitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' 20 V' s mM¹ with 10 μg per 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
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