SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
7th Edition
ISBN: 9781319108236
Author: David L. Nelson, Michael M. Cox
Publisher: W. H. Freeman
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Chapter 17, Problem 9P
Summary Introduction
To explain: The reason that why if palmitate and
Introduction:
The process of fatty acid beta oxidation is completed in different cell organelles. Plamitate which is a saturated fatty acid is activated to palmitoyl-coenzyme A form in cytosol. After which it enters in mitochondria to undergo oxidation.
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12:33
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]
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powered by
desmos
1:30
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:
|||
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:
|||
Chapter 17 Solutions
SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
Ch. 17 - Prob. 1PCh. 17 - Prob. 2PCh. 17 - Prob. 3PCh. 17 - Prob. 4PCh. 17 - Prob. 5PCh. 17 - Prob. 6PCh. 17 - Prob. 7PCh. 17 - Prob. 8PCh. 17 - Prob. 9PCh. 17 - Prob. 10P
Ch. 17 - Prob. 11PCh. 17 - Prob. 12PCh. 17 - Prob. 13PCh. 17 - Prob. 14PCh. 17 - Prob. 15PCh. 17 - Prob. 16PCh. 17 - Prob. 17PCh. 17 - Prob. 18PCh. 17 - Prob. 19PCh. 17 - Prob. 20PCh. 17 - Prob. 21PCh. 17 - Prob. 22PCh. 17 - Prob. 23PCh. 17 - Prob. 24PCh. 17 - Prob. 25PCh. 17 - Prob. 26PCh. 17 - Prob. 27PCh. 17 - Prob. 28PCh. 17 - Prob. 29DAP
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- 12:36 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_forwardProblem 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_forward
- 12:33 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_forward12:33 CO Problem 7 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 Vmax. Report your answer to three significant figures. 1 , mM-1 1 [S] 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: ||| Гarrow_forward
- 12:33 CO Problem 5 of 15 4G 54% Done On the following Lineweaver-Burk 1 plot, identify the by dragging the Vmax point to the appropriate value on the line. NI 35 30- 25 20- 15- 10 5. 1 Vmax -15 10 -5 0 5 10 15 20 20 ||| で Г 25 30 1/[S]arrow_forward12:20 V 0.1- 0:09. 0.08 0:07 0.06 -0.05- 0:04- -0.03- -0.02- 4G 56% Problem 1 of 15 Done On the following Michaelis-Menten plot, estimate the value of - Vmax by 1 2 dragging the line to the appropriate value on the y-axis. 0.01 V max 0 0.5 ||| 1.5 2.5 3.5 4 ISLarrow_forward12:33 CO 4G 54% Problem 6 of 15 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 Km. 1 mM-1 1 [S]' " s mM-1 V 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_forward
- V 0.1- 0:09 0:08 0:07- -0.06 -0.05 0:04- 0:03 0:02 0:01- Problem 2 of 15 Done On the following Michaelis-Menten plot, estimate the value of Kм by dragging the point to the appropriate value on the x-axis. I T | 0 0.5 1.5 2 KM -0:01- ||| 25 2.5 3 3.5 4 Г [S] powered by desmosarrow_forward9. Sketch NMR of the following compound. Clearly label each H-atom in the molecule and where it appears in your NMR. Clearly label the splitting (coupling) pattern (singlet, doublet etc) for each set of equivalent protons. For each signal, clearly label the integration value or the number of protons represented by the signal. Brarrow_forwardPlease help with this Mass Spectrometry Question. Thank you For the mass spec. shown in the attached image, please determine and give the amino acid sequence of the pentapeptide. Show which end is the amino terminus and which is the carboxy terminus. How does one arrive at the solution?arrow_forward
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