FUNDAMENTALS OF BIOCHEMISTRY - LL FD
5th Edition
ISBN: 9781119598022
Author: Voet
Publisher: WILEY
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Chapter 7, Problem 27CQ
Summary Introduction
To explain: A normal individual is incapacitated when exposed to carbon monoxide sufficient enough to occupy the heme sites whereas anemic individual, whose blood has only half the normal Hb content, appears to be in good health.
Concept introduction: Carbon monoxide poisoning occurs when the individual inhales excess carbon monoxide. Carbon monoxide is toxic to cells. Anemia is a condition where there is a reduction in the total number of red blood cells (RBC) and the hemoglobin present in the red blood cells. The T state is the deoxyhemoglobin conformation and R state is the oxyhemoglobin conformation.
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Chapter 7 Solutions
FUNDAMENTALS OF BIOCHEMISTRY - LL FD
Ch. 7 - Prob. 1ECh. 7 - 2. Which set of binding data is likely to...Ch. 7 - Prob. 3ECh. 7 - Prob. 4ECh. 7 - 5. Drinking a few drops of a commercial...Ch. 7 - 6. Explain why long-distance runners prefer to...Ch. 7 - Prob. 7ECh. 7 - Prob. 8ECh. 7 - Prob. 9ECh. 7 - 10. In the variant hemoglobin C, glutamate at...
Ch. 7 - 11. Is myosin a fibrous protein or a globular...Ch. 7 - 12. In striated muscle, cells undergo mitosis...Ch. 7 - 13. A myosin head can undergo five ATP hydrolysis...Ch. 7 - 14. Rigor mortis, the stifle rung of muscles after...Ch. 7 - Prob. 15ECh. 7 - 16. Antibodies are well suited for recognizing...Ch. 7 - 17. Give the approximate molecular masses of an...Ch. 7 - 18. Many fish produce a tetrameric IgM. If each H...Ch. 7 - 19. Explain why the variation in VL and VH domains...Ch. 7 - 20. How many hypervariable loops are present in...Ch. 7 - Prob. 21CQCh. 7 - 22. If myoglobin had the same p50 value as...Ch. 7 - Prob. 23CQCh. 7 - Prob. 24CQCh. 7 - Prob. 25CQCh. 7 - Prob. 26CQCh. 7 - Prob. 27CQCh. 7 - Prob. 28CQCh. 7 - 29. Explain why a microfilament is polar, whereas...Ch. 7 - Prob. 30CQCh. 7 - Prob. 31CQCh. 7 - Prob. 32CQCh. 7 - Prob. 33CQCh. 7 - Prob. 34CQCh. 7 - MORE TO EXPLORE (a) Lock up information about...
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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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