Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 14, Problem 17P
Interpretation Introduction
To propose:
To propose hypothesis that best explains that at 35oC, the
Introduction:
At 35oC, the rate of reaction catalyzed by enzyme A begins to level off.
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Biochemistry
Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 3PCh. 14 - Prob. 4PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 6PCh. 14 - Prob. 7PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οf this...Ch. 14 - Answers to all problems are at the end οf this...
Ch. 14 - Answers to all problems are at the end of this...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 14PCh. 14 - Prob. 15PCh. 14 - Prob. 16PCh. 14 - Prob. 17PCh. 14 - Prob. 18PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 22PCh. 14 - Prob. 23PCh. 14 - Prob. 24PCh. 14 - Prob. 25PCh. 14 - Prob. 26P
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- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.arrow_forwardAnswers to all problems are at (he end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Understanding State Functions Define a slate function. Name three thermodynamic quantities that are state functions and three thatarrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. General Controls Over Enzyme Activity List six general ways in which enzyme activity is controlled.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of MWC Allosteric Enzyme Kinetics (Integrates with Chapter 1.1) Draw both Line weaver-Burk plots and Hanes-Woolf plots for an MWC allosteric enzyme system, showing separate curves for the kinetic response in (a) the absence of any effectors, (b) the presence of allosteric activator Λ, and (c) the presence of allosteric inhibitor I.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of Negative Gooperativity in KNF Allosteric Enzyme Kinetics The KNF model for allosteric transitions includes the possibility of negative cooperativity Draw Lineweaver-Burk and Hanes-Woolf plots for the case of negative cooperatively m substrate binding. (As a point of reference, include a line showing the classic Michaelis-Menten response of v to [S].)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. CalculatingGandSfromH The equilibrium constant for some process AB 0.5 at 20°C and 10 at 30°C. Assuming that G is independent of temperature, calculate H for this reaction. GandSat20Candat30C Why- is it important in this problem to assume that H is independent of temperature?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. How Varying the Amount of Enzyme or the Addition of Inhibitors Affects v Versus [S] Plots Using Figure 13.7 as a model, draw curves that would be obtained in v versus [S] plots when a. twice as much enzyme is used. b. half as much enzyme is used. c. a competitive inhibitor is added. d. a pure noncompetitive inhibitor is added. e. an uncompetitive inhibitor is added. For each example, indicate how Vmax and Km change.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Exploring the Michaelis-Menten Equation - II If Vmax=100mol/mLsecand Km=2mM, what is the velocity of the reaction when [S] = 20 mM?arrow_forwardAnswers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Calculation of Rate Enhancement from Energies of Activation The relationships between the free energy terms defined in the solution to Problem 4 earlier are shown in the following figure. If the energy of the ES complex is 10 kJ/mol lower than the energy of E + S, the value of Ge:is 20 kJ/mol, and the value of Ge:is 90 kJ/mol what is the rate enhancement achieved by an enzyme in this case?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Cells as Steady-State Systems Describe what is meant by the phrase "cells tire steady-state systems." (Section 1.4)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Assessing the Chemistry and Enzymology of “Light Beer� Biochemist Joseph Owades revolutionized the production of beer in the United States by developing a simple treatment with an enzyme that converted regular beer into “light beer, which was marketed aggretssively as a beverage that tastes great, even though it is less filling. What was the enzyme-cataIyzed reaction that Owades used to modify the fermentation process so cleverly, and how is regular beer different from light beer?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - I Measurement of the rate constants for a simple enzymatic reaction obeying Michaelis-Menten kinetics gave the following results: k1=2108M1sec1k1=1103sec1k2=5103sec1a. What is Ks, the dissociation constant for the enzyme-substrate complex? b. What is Km, the Michaelis constant for this enzyme? c. What is kcat (the turnover number) for this enzyme? d. What is the catalytic efficiency (kcat/Km) for this enzyme? e. Does this enzyme approach kinetic perfection? (That is, does kcat/Km approach the diffusion-controlled rate of enzyme association with substrate?) f. If a kinetic measurement was made using 2 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? g. Again, using 2 nanomoles of enzyme per mL of reaction mixture, what concentration of substrate would give v = 0.75 Vmax? h. If a kinetic measurement was made using 4 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? What would Km equal under these conditions?arrow_forward
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