FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
5th Edition
ISBN: 9781119750192
Author: Voet
Publisher: WILEY
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Chapter 6, Problem 33CQ
Summary Introduction
To calculate: The ratio of the volume of a hemoglobin molecule (65 kD) of the four O2 molecules that bind and the ratio of the volume of a typical office (4×4×3m) of the typical (70-Kg) office worker that occupies it.
Summary Introduction
To compare: The ratio of volume of a hemoglobin molecule (65 kD) of the four O2 molecules in equal proportions to their molecular masses in office (4×4×3m) and that the office worker has a density of 1.0 g/cm3 and check if it matches with the expected results.
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Chapter 6 Solutions
FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
Ch. 6 - Prob. 1ECh. 6 - Prob. 2ECh. 6 - 3. Why would you be unlikely to see an ? helix...Ch. 6 - 4. Calculate the length in angstroms of a...Ch. 6 - Prob. 5ECh. 6 - 6. Collagen IV, which occurs in basement...Ch. 6 - 7. Describe the primary, secondary, tertiary, and...Ch. 6 - 8. Explain why gelatin, which is mostly collagen,...Ch. 6 - Prob. 9ECh. 6 - 10. Is it possible for a native protein to be...
Ch. 6 - Prob. 11ECh. 6 - 12. (a) Is Trp or Gln more likely to be on a...Ch. 6 - 13. Classify the following proteins as ?, ?, or...Ch. 6 - 14. Classify the following proteins as ?, ?, or...Ch. 6 - 15. You are performing site-directed mutagenesis...Ch. 6 - 16. Laboratory techniques for randomly linking...Ch. 6 - Prob. 17ECh. 6 - 18. The genetically engineered proteins that...Ch. 6 - Prob. 19ECh. 6 - 20. Experiments in mice suggest that...Ch. 6 - 21. Helices can be described by the notation nm,...Ch. 6 - Prob. 22CQCh. 6 - 23. Which of the following polypeptides is most...Ch. 6 - 24. Which of the peptides in Problem 23 is least...Ch. 6 - Prob. 25CQCh. 6 - 26. What types of rotational symmetry are possible...Ch. 6 - Prob. 27CQCh. 6 - 28. Proteins in solution are often denatured if...Ch. 6 - 29. Given enough time, will all denatured proteins...Ch. 6 - Prob. 30CQCh. 6 - 31. Under physiological conditions, polylysine...Ch. 6 - 32. Would intrinsically disordered polypeptide...Ch. 6 - Prob. 33CQCh. 6 - Prob. 34CQCh. 6 - Prob. 35CQCh. 6 - 36. Not all heat shock proteins are chaperones;...Ch. 6 - 37. Protein denaturation can be triggered by a...Ch. 6 - 38. Explain why ? sheets are less likely to form...Ch. 6 - 39. The GroEL/ES cycle diagrammed in Fig. 6-45...Ch. 6 - Prob. 1MTE
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Similar questions
- 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
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