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Concept explainers
Interpretation:
Concept Introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino functional group is
Zwitter ion has both positive as well as negative charge, thus it is also called neutral dipolar ion.
Zwitter ion accepts proton in acidic condition and in basic condition zwitter ion lose electrons.
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Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
- 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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