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Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 3, Problem 28CQ
Summary Introduction
To determine: The pK value of N3 in cytosine and in uracil.
Concept introduction:
The strength of an acid is expressed as its pK value. It is defined as the negative logarithm of equilibrium constant. The pK value depends on the pH value, stronger is the acid, lower its pK value. The pK value of
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Chapter 3 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 3 - Prob. 1ECh. 3 - 2. Name the following nucleotide.
Ch. 3 - 3. In many organisms, DNA is modified by...Ch. 3 - 4. When cytosine is treated with bisulfite, the...Ch. 3 - 5. Kinases are enzymes that transfer a phosphoryl...Ch. 3 - 6. Kinases are enzymes that transfer a phosphoryl...Ch. 3 - 7. A diploid organism with a 45,000-kb haploid...Ch. 3 - 8. A segment of DNA containing 20 base pairs...Ch. 3 - 9. Explain why the strands of a DNA molecule can...Ch. 3 - 10. Explain why increasing the NaCl concentration...
Ch. 3 - 11. An enzyme from the human immunodeficiency...Ch. 3 - 12. How many different amino acids could...Ch. 3 - 13. The human genome contains thousands of...Ch. 3 - 14. By how many nucleotides, on average, do the...Ch. 3 - 15. The recognition sequence for the restriction...Ch. 3 - 16. Using the data in Table 3-2, identify...Ch. 3 - 17. The 13-Mb genome of the green alga...Ch. 3 - 18. Describe how to select recombinant clones if a...Ch. 3 - Prob. 19ECh. 3 - Prob. 20ECh. 3 - 21. Why is a genomic library larger than a cDNA...Ch. 3 - 22. Why do cDNA libraries derived from different...Ch. 3 - 23. Some RNA molecules me covalently modified by...Ch. 3 - 24. Would the modified nucleoside described in...Ch. 3 - 25. Draw the tautomeric form of adenine.
Ch. 3 - 26. Draw the tautomeric form of cytosine.
Ch. 3 - 27. The pK value for N1 of adenine is 3.64,...Ch. 3 - Prob. 28CQCh. 3 - Prob. 29CQCh. 3 - 30. Hypoxanthine can also base-pair with cytosine....Ch. 3 - 31. Describe the outcome of a chain-terminator...Ch. 3 - 32. Describe the outcome of a chain-terminator...Ch. 3 - 33. Calculate the number of clones required to...Ch. 3 - 34. You are attempting to clone a 250-kb segment...Ch. 3 - 35. Describe the possible outcome of a PCR...Ch. 3 - 36. Describe the possible outcome of a PCR...Ch. 3 - 37. Write the sequences of the two 12-residue...Ch. 3 - 38. A blood slain from a crime scene and blood...Ch. 3 - 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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