Proteins are thermodynamically unstable molecules since the Delta G of hydrolysis is quite negative. However, most proteins are not degraded unless they come into contact with proteases in cells. What is the reasoning for this paradox? The reaction is endergonic and will not proceed without energy. There is very little water inside cells to react with protein molecules. The free energy change doesn't reveal anything about the rate of the reaction. The concentration of proteins are low which allows them to be more stable.

Chemistry: Principles and Reactions
8th Edition
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:William L. Masterton, Cecile N. Hurley
Chapter23: Organic Polymers, Natural And Synthetic
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Proteins are thermodynamically unstable molecules since the Delta G of hydrolysis is
quite negative. However, most proteins are not degraded unless they come into
contact with proteases in cells. What is the reasoning for this paradox?
The reaction is endergonic and will not proceed without energy.
There is very little water inside cells to react with protein molecules.
The free energy change doesn't reveal anything about the rate of the reaction.
The concentration of proteins are low which allows them to be more stable.
Transcribed Image Text:Proteins are thermodynamically unstable molecules since the Delta G of hydrolysis is quite negative. However, most proteins are not degraded unless they come into contact with proteases in cells. What is the reasoning for this paradox? The reaction is endergonic and will not proceed without energy. There is very little water inside cells to react with protein molecules. The free energy change doesn't reveal anything about the rate of the reaction. The concentration of proteins are low which allows them to be more stable.
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