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Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 8, Problem 18E
Summary Introduction
To identify: The amino-acids that are abundant in the fibroblast growth factor.
Concept introduction:
Growth factors are the heterogeneous group of polypeptides or proteins. They are signaling molecules. They act through specific receptors of cells and triggers secondary messengers that lead to cell proliferation. They stimulate cell division, differentiation, growth and survival. The fibroblast growth factor belongs to the family of peptide cytokines. They have a well-built chemoattractant and mitogenic activity for the epithelial cells and can also help for the regulation of many tissues.
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Students have asked these similar questions
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:
|||
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
Г
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:
|||
Chapter 8 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 8 - Prob. 1ECh. 8 - 2. Are (a) d-glucitol, (b) d-galactitol, and (c)...Ch. 8 - 3. Which of the following pairs of sugars are...Ch. 8 - 4. Which of the following pairs of sugars are...Ch. 8 - 5. Draw the furanose and pyranose forms of...Ch. 8 - 6. Draw a Fischer projection of l-fucose. l-Fucose...Ch. 8 - 7. Some bacteria produce thiosugars, which contain...Ch. 8 - 8. The metabolism of monosaccharides yields...Ch. 8 - 9. The sucrose substitute tagatose (Fig. 8-2) is...Ch. 8 - 10. What type of sugar derivative is rhamnose?
Ch. 8 - 11. Draw the structure of the mannose...Ch. 8 - 12. Identify the monosaccharides and their...Ch. 8 - 13. How many reducing ends are in a molecule of...Ch. 8 - 14. Is amylose or amylopectin more likely to be a...Ch. 8 - Prob. 15ECh. 8 - 16. The core of pectin molecules is a polymer of...Ch. 8 - 17. Calculate the net charge of a...Ch. 8 - Prob. 18ECh. 8 - 19. In certain situations, a glycosyltransferase...Ch. 8 - Prob. 20ECh. 8 - 21. Draw the structure of the O-type...Ch. 8 - 22. During gel electrophoresis, glycoproteins...Ch. 8 - 23. How many different disaccharides of...Ch. 8 - 24. In addition to lactose, how many other...Ch. 8 - 25. (a) Deduce the structure of the disaccharide...Ch. 8 - 26. The artificial sweetener sucralose is a...Ch. 8 - 27. Broun algae produce alginate, a polysaccharide...Ch. 8 - 28. Human milk contains the oligosaccharide...Ch. 8 - 29. Cellulose is treated with methanol, which...Ch. 8 - 30. Glycogen is treated with dimethyl sulfate,...Ch. 8 - 31. Following their synthesis, many proteoglycans...Ch. 8 - 32. The peptidoglycan cell walls of bacteria...Ch. 8 - Prob. 33CQCh. 8 - 34. One demonstration of P.T. Barnum’s maxim that...Ch. 8 - MORE TO EXPLORE Chitosan is a substance produced...
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Similar questions
- 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
- 12:33 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_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_forward
- 12:33 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_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_forward
- Please 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_forward2. For the flow of fluid over a flat membrane of length 10cm, determine the length-average mass transfer coefficient. The relevant properties of the system are u=0.01cm²/s, D=5 x 106 cm²/s, and v = 5.0 cm/s.arrow_forward
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