Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 5, Problem 5.12PS
(a)
Summary Introduction
To prove: The equilibrium constant K’AD for the overall reaction is the product of the three component equilibrium constants for the given reaction:
K’AB, K’BC, and K’CD are the respective equilibrium constants for reaction
Introduction: In a system, multiple
(b)
Summary Introduction
To prove: For the overall conversion of A to D,
Introduction: In a system, multiple chemical reactions can take place at the same time. Each of the proceeding reactions has their own thermodynamic parameters such as enthalpy, free energy and others. If these reactions take place in a sequential manner and are a part of a bigger chemical process, then the total free energy for the complete system can be calculated using the free energies of the individual reactions.
(c)
Summary Introduction
To prove: The
Introduction: In a system, multiple chemical reactions can take place at the same time. Each of the proceeding reactions has their own thermodynamic parameters such as enthalpy, free energy and others. If these reactions take place in a sequential manner and are a part of a bigger chemical process, then the total free energy for the complete system can be calculated using the free energies of the individual reactions.
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ch
Select all statements that are correct. Note there might be more than 1 correct
statement.
From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained
The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis-
Menten plot
The Lineweaver-Burk plot assumes that products and reactants are present at equal
concentrations during the entire time of the reaction
The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration
The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration
O
20°C
D)
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E
X Incorrect.
Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the
reaction? Choose all that are correct.
The enzyme increases the AG value.
The enzyme increases the rate of reaction.
The enzyme decreases the rate of reaction.
The enzyme decreases the AG value.
The enzyme raises the activation energy.
The enzyme lowers the activation energy.
Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?
Chapter 5 Solutions
Becker's World of the Cell (9th Edition)
Ch. 5 - How do phototrophs and chemotrophs depend...Ch. 5 - How does the spontaneity of a chemical reaction...Ch. 5 - QUESTION: Why does the height of the spike get...Ch. 5 - For a chemical reaction happening in a cell, what...Ch. 5 - Prob. 5.1PSCh. 5 - QUANTITATIVE Photosynthetic Energy Transduction....Ch. 5 - Energy Conversion. Most cellular activities...Ch. 5 - Problem Set Enthalpy, Entropy, and Free Energy....Ch. 5 - Violating the Second Law? The second law of...Ch. 5 - QUANTITATIVE The Equilibrium Constant. The...
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- . Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?arrow_forwardnot true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forwarda. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "arrow_forward
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