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Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 31, Problem 34P
Interpretation Introduction
Interpretation:
The differences between the bacterial and eukaryotic protein synthesis should be determined.
Concept introduction:
Protein synthesis (translation) is a process of generating new protein sequences inside the cell. This process takes place in the cytoplasm of the cell. This process is balanced by the degradation or export of cellular proteins. It is constituted of three steps namely, initiation, elongation, and termination.
Expert Solution & Answer
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Students have asked these similar questions
Problem 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:
|||
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:
|||
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:
|||
Г
Chapter 31 Solutions
Biochemistry
Ch. 31 - Prob. 1PCh. 31 - Prob. 2PCh. 31 - Prob. 3PCh. 31 - Prob. 4PCh. 31 - Prob. 5PCh. 31 - Prob. 6PCh. 31 - Prob. 7PCh. 31 - Prob. 8PCh. 31 - Prob. 9PCh. 31 - Prob. 10P
Ch. 31 - Prob. 11PCh. 31 - Prob. 12PCh. 31 - Prob. 13PCh. 31 - Prob. 14PCh. 31 - Prob. 15PCh. 31 - Prob. 16PCh. 31 - Prob. 17PCh. 31 - Prob. 18PCh. 31 - Prob. 19PCh. 31 - Prob. 20PCh. 31 - Prob. 21PCh. 31 - Prob. 22PCh. 31 - Prob. 23PCh. 31 - Prob. 24PCh. 31 - Prob. 25PCh. 31 - Prob. 26PCh. 31 - Prob. 27PCh. 31 - Prob. 28PCh. 31 - Prob. 29PCh. 31 - Prob. 30PCh. 31 - Prob. 31PCh. 31 - Prob. 32PCh. 31 - Prob. 33PCh. 31 - Prob. 34PCh. 31 - Prob. 35PCh. 31 - Prob. 36PCh. 31 - Prob. 37PCh. 31 - Prob. 38PCh. 31 - Prob. 39PCh. 31 - Prob. 40PCh. 31 - Prob. 41PCh. 31 - Prob. 42PCh. 31 - Prob. 43PCh. 31 - Prob. 44PCh. 31 - Prob. 45PCh. 31 - Prob. 46PCh. 31 - Prob. 47PCh. 31 - Prob. 48PCh. 31 - Prob. 49PCh. 31 - Prob. 50PCh. 31 - Prob. 51PCh. 31 - Prob. 52P
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- 1:33 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_forward12:33 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_forward
- 12:20 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_forwardV 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_forward
- 9. 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_forwardDraw a tripeptide of your choosing at pH 7. Have the N-terminus on the left and the C-terminus on the right. Then: Draw a triangle around the α-carbons. Draw a box around the R-groups. Circle the atoms capable of hydrogen bonding. Highlight the atoms involved in the formation of the peptide bonds. What type of structure have you drawn? (primary, secondary, tertiary or quaternary protein structure).arrow_forward
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