Question

In: Chemistry

This is a very simpllistic approach to protein folding, which ignores solvent and volume effects, but...

This is a very simpllistic approach to protein folding, which ignores solvent and volume effects, but it allows us to practice what we have learned about thermodynamics and kinetics. Enzymes are long chains of amino acids that have to fold in the proper way so as to exhibit enzyme activity. They can catalyze certain reactions. Let us pick a reaction in the human body at 37 C, we will call it enzyme X.

Let's say that enzyme X is the catalyst responsible for breaking starch down to individual glucose molecules. What of the following things can happen to the starch and enzyme system if you rainse the temperature?

a-the rate of the reaction of starch going to glucose will increase

b-nothing should happen since a catalyst does not affect the equilibrium

c-the enzyme could stop working effectively becauset the folded form would stop being made and would start to unravel if the process is reversible

d-the equilibrium constant will get bigger to favor the glucose side more

Solutions

Expert Solution

Here (c) would be the correct answer i.e. the enzyme could stop working effectively because the folded form would stop being made and would start to unravel if the process is reversible. Because enzyme action in our body is temperature and PH dependent. The enzyme activity is maximum at optimum temperature( normally the body temperature) and optimum PH range( usually 5-7). Because at optimum temperature, they are in their right shape with proper folding of aminoacid chains catalysing the reaction at optimum rate.

However when the temperature is decreased, the enzyme becomes too tight losing its proper shape and hence decreases the enzyme activity. Also when the temperature is increased,the enzyme becomes too lose losing its shape. This also decreases the enzyme to a great extent. If the temperature increase or decrease it too large, the enzyme becomes denatured losing its function completely.


Related Solutions

Outline requirements for correct protein folding
Outline requirements for correct protein folding
27. Which of the following statements is not true concerning protein folding? a. Proteins fold around...
27. Which of the following statements is not true concerning protein folding? a. Proteins fold around a hydrophobic core b. The interior of proteins is held together exclusively by hydrophobic interactions c. The amino acid sequence of a protein is responsible for determining the shape of a protein d. The active conformation of a protein is it most thermodynamically favorable state e. none of the above
The hydrophobic effect is the primary driving force for protein folding because A) a folded protein...
The hydrophobic effect is the primary driving force for protein folding because A) a folded protein maximizes the entropy of water B) an unfolded protein maximizes the entropy of a biological system C) a folded protein is able to form the most hydrogen bonds D) hydrogen bonds within the protein replace hydrogen bonds between the protein and water
7. Discuss the primary issues associated with protein folding.
7. Discuss the primary issues associated with protein folding.
Describe in comeplete detail the anfinsen experiment in protein folding.
Describe in comeplete detail the anfinsen experiment in protein folding.
Describe the likely order of events for the folding of a globular protein and why is...
Describe the likely order of events for the folding of a globular protein and why is this sequence of events likely? What is the chemical/physical rationale for each step? Include a brief discussion of Levinthal’s paradox.
How do the 4 levels of protein folding relate to one another?
How do the 4 levels of protein folding relate to one another?
We discussed that the main driving force for protein folding (in an aqueous environment) is the...
We discussed that the main driving force for protein folding (in an aqueous environment) is the hydrophobic effect. Using a thermodynamic analysis explain why this is the case. You analysis should take in to account the peptide bonds, polar side chains, non-polar side chains, the influence of solvent water, and the enthaplic and entropic contributions of each of these.
23. What role does aberrant protein folding play in the development of a disease such as...
23. What role does aberrant protein folding play in the development of a disease such as Alzheimer’s disease?
In the Anfinsen protein folding experiment the sequence of removing urea or BME makes a difference...
In the Anfinsen protein folding experiment the sequence of removing urea or BME makes a difference for functional refolding of the protein. Explain why removing BME first leads to a nonfunctional enzyme, but removing urea first leads to a functional enzyme. Why does adding small amounts of BME alone to the solution with the nonfunctional enzyme "rescue" the function biochemistry
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT