BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 31, Problem 37P
Interpretation Introduction
Interpretation:
The given columns should be matched.
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, initiation, elongation, and termination.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
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-ACHIEVE (1 TERM)
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
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- 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
- 2. 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_forwardBackground Freezing isn't the only challenge in cryopreservation - thawing can be just as difficult. A microwave oven seems like a nice solution, since it deposits energy quickly and microwaves are non-ionizing radiation (they do not cause DNA mutation). However, water absorbs microwaves more effectively than ice does, meaning that the portion of an organ that has already melted will get warmer at a higher rate than the remaining ice – the opposite of what we want! - The transmission of radiation through a weakly absorbing material such as ice or water can be modeled by Beer's law, which assumes that the rate of absorption at a depth x is proportional to the local radiation intensity I(x) times an absorption coefficient, which is often written as μ or a or just µ). Noting that absorption decreases the intensity, we can write a differential equation a Solving the differential equation with the boundary condition on the surface being gives the relationship For a standard microwave oven…arrow_forward3. Dry air is inhaled at a rate of 10 liter/min through a trachea with a diameter of 20 mm and a length of 125 mm. The inner surface of the trachea is at a normal body temperature of 37°C and may be assumed to be saturated with water. a. Assuming steady, fully developed flow in the trachea, estimate the mass transfer convection coefficient. b. Estimate the daily water loss (liter/day) associated with evaporation in the trachea.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Principles Of Radiographic Imaging: An Art And A ...Health & NutritionISBN:9781337711067Author:Richard R. Carlton, Arlene M. Adler, Vesna BalacPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Understanding Nutrition (MindTap Course List)Health & NutritionISBN:9781337392693Author:Eleanor Noss Whitney, Sharon Rady RolfesPublisher:Cengage Learning
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Principles Of Radiographic Imaging: An Art And A ...
Health & Nutrition
ISBN:9781337711067
Author:Richard R. Carlton, Arlene M. Adler, Vesna Balac
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Understanding Nutrition (MindTap Course List)
Health & Nutrition
ISBN:9781337392693
Author:Eleanor Noss Whitney, Sharon Rady Rolfes
Publisher:Cengage Learning
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax