Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Textbook Question
Chapter 8, Problem 3IQ
Develop a concept map on free energy and ΔG. The value in this exercise is for you to wrestle with and organize these concepts for yourself. Do not turn to the suggested concept map until you have worked on your own understanding. Remember that the concept map in the answer section is only one way of structuring these ideas—have confidence in your own organizational scheme.
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Students have asked these similar questions
A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are
shown below:
Vo (mM/min)
(without inhibitor)
Vo (mM/min)
(with inhibitor)
[Substrate]
(mM)
15
1.11
0.67
30
1.81
1.17
45
2.28
1.56
60
2.62
1.88
90
3.09
2.36
Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the ab-
sence of an inhibitor.
- y-int =
- slope =
- vmax =
- Km =
Hi! Please may I have a detailed solution for this question. You need to design a fully detailed mindmap to show how to reduce food waste in a home or workplace, so option (a)
Match each inhibitor with its effect on Michaelis-Menten reactions.
Group of answer choices
Vmax and apparent Vmax are equal and the apparent Km is greater than Km.
The apparent Vmax is less than Vmax and the apparent Km and Km are equal
The apparent Vmax and the apparent Km are both lowered to the same degree.
The apparent Vmax is less than Vmax and the apparent Km can be either greater than or less than Km.
Chapter 8 Solutions
Study Guide for Campbell Biology
Ch. 8 - Complete the following concept map that summarizes...Ch. 8 - Complete the following table to indicate how the...Ch. 8 - Develop a concept map on free energy and G. The...Ch. 8 - Prob. 4IQCh. 8 - Prob. 5IQCh. 8 - In the following graph of an exergonic reaction...Ch. 8 - In the following diagram of a catalytic cycle,...Ch. 8 - Return to the diagram in Interactive Question 3.7,...Ch. 8 - Both ATP and ADP serve as regulators of enzyme...Ch. 8 - What is the relationship between the concept of...
Ch. 8 - What role do enzymes play in metabolism?Ch. 8 - ________ the totality of an organisms chemical...Ch. 8 - _______ pathways that use energy to synthesize...Ch. 8 - Prob. 3TYKFCh. 8 - _______ the most random form of energyCh. 8 - _______ term for the measure of disorder or...Ch. 8 - Prob. 6TYKFCh. 8 - _______ inhibitors that decrease an enzymes...Ch. 8 - Prob. 8TYKFCh. 8 - Prob. 9TYKFCh. 8 - Prob. 10TYKFCh. 8 - Catabolic and anabolic pathways are often coupled...Ch. 8 - Which statement most closely reflects the first...Ch. 8 - When a cell breaks down glucose, only about 34% of...Ch. 8 - Prob. 4TYKCh. 8 - Prob. 5TYKCh. 8 - Prob. 6TYKCh. 8 - One way in which a cell maintains metabolic...Ch. 8 - Prob. 8TYKCh. 8 - Prob. 9TYKCh. 8 - What is meant by an induced fit? a. The binding of...Ch. 8 - In an experiment, changing the pH from 7 to 6...Ch. 8 - Prob. 12TYKCh. 8 - Penicillin binds to the active site of an enzyme...Ch. 8 - Prob. 14TYKCh. 8 - Prob. 15TYKCh. 8 - Which line in the diagram indicates the G of the...Ch. 8 - Prob. 17TYKCh. 8 - Prob. 18TYKCh. 8 - Prob. 19TYKCh. 8 - Prob. 20TYK
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- Regarding the reasoning for the Michaelis-Menten equation to be unsuitable for accurate analysis of experimental data, select all that apply: It is nonlinear It is only valid for reactions at equilibrium It is not valid under experimental conditions Extrapolation to Vm is inaccurate and therefore Km also cannot be accurately describedarrow_forwardA biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: [Substrate] (MM) 10 30 50 70 ▪ slope = ▪ Vmax= ▪ Km = Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor. ▪y-int= [Select] [Select] ▪ Km = [Select] [Select] Vo (mm/min) (without inhibitor) [Select] 4.43 10.26 14.07 16.73 [Select] mM/min mM Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the presence of an inhibitor. ▪ y-int= [Select] ▪ slope = [Select] ▪ Vmax= Vo (mm/min) (with inhibitor) ✓mM/min mM 2.60 6.06 8.23 9.73 What is the type of inhibition involved? [Select]arrow_forwardBriefly compare and discuss (in less than 100 words) the three energy nutrients in terms of their relative roles as fuel in exercise. What are the fuel values of the three energy nutrients? What do these values mean? What is our primary energy nutrient and why?arrow_forward
- Determine the cause-effect relationship of the following variables given. Choose the best answer that describes the possible changes in variable (Y) as a consequence of the changes done to variable (X). Change: Increase in phosphorylation process vs. GCS activity (Y) Cannot be determined Decrease Increase No effectarrow_forwardPlease help me solve this problems.arrow_forwardViruses are not considered to be alive but are still considered cells. True O Falsearrow_forward
- The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor will have the same 1. Vmax2. Km3. Km/Vmax4. 1/Vmaxarrow_forwardAccording to Kleiber’s law, for the vast majority of animals, an animal’s metabolic rate is proportional to m 0.75, where m is the animal’s mass. When we plot the graph of the common logarithm of the mass on the horizontal axis and the common logarithm of the metabolic rate on the vertical axis, we get a straight line. Explain why the graph is a straight line. What is the slope of the line?arrow_forwardYou were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, uM) Vo with DEDS (uM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 2.500 1.923 4.259 3.333 2.139 4.737 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax KMarrow_forward
- Consider the given data for an enzyme-catalyzed reaction. Determine the Vm, Km and the type of inhibition based on the given data below Substrate concentration, uM 30 50 100 300 900 slope y-intercept Complete the table below (include correct units). Experiment A Vm Km Experiment A (Initial velocity without inhibitor, uM-min) Type of Inhibition: 10.4 14.5 22.5 33.8 40.8 Experiment B (Initial velocity with inhibitor, uM-min) 5.1 7.3 13.3 25.7 37.2 Experiment Barrow_forwardCompound A is the substrate for two enzymes, El and E2, their reaction rates, r1 and r2,Determine the Km and rmax for both enzymes, with respect to the concentration of A. Which set of data is more likely to be for El and which for E2, and why? Concentration of 0.2 0.6 1.2 3 4 5 6 8 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80arrow_forwardAcetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) Aarrow_forward
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