Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 15, Problem 53RE
Interpretation Introduction
Interpretation:
The molecular logic that makes a pathway with a number of comparatively small energy changes more likely than the one with a single reaction involving a large energy change is to be discussed.
Concept introduction:
In biochemistry, the
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Biochemistry
Ch. 15 - RECALL Is there a connection between the...Ch. 15 - REFLECT AND APPLY What do the following indicators...Ch. 15 - REFLECT AND APPLY Consider the reaction...Ch. 15 - RECALL What conditions are necessary for the...Ch. 15 - REFLECT AND APPLY Why is it important that energy...Ch. 15 - RECALL Why is it necessary to define a modified...Ch. 15 - RECALL Which of the following statements is (are)...Ch. 15 - RECALL How can you tell if the standard Gibbs free...Ch. 15 - RECALL Can the thermodynamic property G be used to...Ch. 15 - MATHEMATICAL Calculate G for the following values...
Ch. 15 - Prob. 11RECh. 15 - MATHEMATICAL Consider the reaction AB+C, where...Ch. 15 - Prob. 13RECh. 15 - MATHEMATICAL The G for the reaction Citrate ...Ch. 15 - MATHEMATICAL If a reaction can be written AB, and...Ch. 15 - Prob. 16RECh. 15 - Prob. 17RECh. 15 - Prob. 18RECh. 15 - RECALL Organize the following words into two...Ch. 15 - Prob. 20RECh. 15 - REFLECT AND APPLY Would you expect the production...Ch. 15 - Prob. 22RECh. 15 - REFLECT AND APPLY Adult humans synthesize large...Ch. 15 - RECALL Identify the molecules oxidized and reduced...Ch. 15 - RECALL For each of the reactions in Question 24,...Ch. 15 - Prob. 26RECh. 15 - RECALL What is the structural difference between...Ch. 15 - RECALL How does the difference between NADH and...Ch. 15 - RECALL Which coenzyme is a reactant in the...Ch. 15 - Prob. 30RECh. 15 - Prob. 31RECh. 15 - Prob. 32RECh. 15 - REFLECT AND APPLY The following half reactions...Ch. 15 - Prob. 34RECh. 15 - REFLECT AND APPLY There is a reaction in...Ch. 15 - REFLECT AND APPLY There is a reaction in which...Ch. 15 - Prob. 37RECh. 15 - Prob. 38RECh. 15 - Prob. 39RECh. 15 - Prob. 40RECh. 15 - MATHEMATICAL Using the data in Table 15.1,...Ch. 15 - Prob. 42RECh. 15 - Prob. 43RECh. 15 - MATHEMATICAL The standard free-energy change for...Ch. 15 - Prob. 45RECh. 15 - Prob. 46RECh. 15 - Prob. 47RECh. 15 - REFLECT AND APPLY Would you expect an increase or...Ch. 15 - REFLECT AND APPLY Explain and show why...Ch. 15 - Prob. 50RECh. 15 - Prob. 51RECh. 15 - Prob. 52RECh. 15 - Prob. 53RECh. 15 - REFLECT AND APPLY Why are thioesters considered...Ch. 15 - Prob. 55RECh. 15 - REFLECT AND APPLY This is a conjectural question:...
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- REFLECT AND APPLY What is the relationship between a transition-state analog and the induced-fit model of enzyme kinetics?arrow_forwardREFLECT AND APPLY What do the following indicators tell you about whether a reaction can proceed as written? (a) The standard free-energy change is positive. (b) The free-energy change is positive. (c) The reaction is exergonic.arrow_forwardREFLECT AND APPLY Comment on the energetics of protein folding in light of the information in this chapter.arrow_forward
- REFLECT AND APPLY The process of protein folding is spontaneous in the thermodynamic sense. It gives rise to a highly ordered conformation that has a lower entropy than the unfolded protein. How can this be?arrow_forwardREFLECT AND APPLY Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by non-covalent interactions? Why?arrow_forwardREFLECT AND APPLY Would nature rely on the same enzyme to catalyze a reaction either way (forward or backward) if the DG were 0.8kcalmol1? If it were 5.3kcalmol1?arrow_forward
- REFLECT AND APPLY Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?arrow_forwardREFLECT AND APPLY A model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?arrow_forwardREFLECT AND APPLY Suggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is the decrease of activity frequently much less when the solution contains high concentrations of the substrate?arrow_forward
- REFLECT AND APPLY The enzyme D-amino acid oxidase has a very high turnover number because the D-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to 2 mM for the aromatic amino acids and in the range of 15 to 20 mM for such amino acids as serine, alanine, and the acidic amino acids. Which of these amino acids are the preferred substrates for the enzyme?arrow_forwardREFLECT AND APPLY Would you expect the structure of a non- competitive inhibitor of a given enzyme to be similar to that of its substrate?arrow_forwardREFLECT AND APPLY When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?arrow_forward
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