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Multiple Choice
Considering that peptide bond hydrolysis is exergonic, how is the stability of a peptide bond accounted for?
A
Despite the thermodynamic favorability of hydrolysis, peptide bond formation is more favorable.
B
The numerous peptide bonds in a typical protein synergistically make hydrolysis unfavorable.
C
Peptide bonds are only stable and avoid hydrolysis in cellular environments.
D
Though peptide bond hydrolysis is thermodynamically favorable, there is a high energy of activation.
Verified step by step guidance
1
Understand the concept of peptide bond hydrolysis: Peptide bonds link amino acids in proteins and their hydrolysis is the process of breaking these bonds, which is thermodynamically favorable (exergonic).
Recognize the role of activation energy: Despite the thermodynamic favorability, peptide bond hydrolysis requires overcoming a high energy barrier, known as the activation energy, which makes the process slow under normal conditions.
Consider the cellular environment: In living organisms, peptide bonds are stable because the cellular environment does not provide the necessary conditions to overcome the activation energy easily.
Explore the role of enzymes: Enzymes such as proteases can lower the activation energy required for hydrolysis, allowing the process to occur more readily when needed, such as during protein digestion.
Reflect on protein stability: The stability of proteins is maintained by the high activation energy barrier, ensuring that proteins do not spontaneously degrade, despite the thermodynamic favorability of peptide bond hydrolysis.