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The linear sequence of amino acids is referred to as the primarylevel of protein structure. However, the primary sequence affectsall other aspects of protein structure.

a. Explain how an amino acidchange outside of the active site of a particular enzyme couldaffect the function of that enzyme. (2pts)

b. Explain how that same aminoacid change could have no affect on the function of the enzyme.(2pts)

c. Imagine a protein in which acysteine is converted to a serine. How would this mutation affectthe secondary, tertiary and quaternary structure? (3pts)

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28 Sep 2019
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Related questions

1) Enzymes are important biological molecules that we have discussed through this course. Describe how the structure of an enzyme can contribute to its specific function within a cell.

a) Dicuss several factors/conditions that could modify the structure and/or function of an enzyme using specific examples (i.e beta-galactosidase/lactase).

b) At the tertiary or quaternary level of organization what would happen if a mutation were to occur in the primary protein sequence coding for an enzyme? Describe different types of mutations that can occur in the protein sequence and how would this affect the different levels of protein folding (structure) and the activity of the enzyme (function)? Remember hemoglobin and what occurs in Sickle cell disease.

1. Enzyme A is an enzyme that catalyzes the reaction of glucose + fructose to sucrose by coupling this +∆G reaction with the -∆G hydrolysis of ATP. A chemical is discovered that keeps Enzyme A from entering its transition state. What will happen when this enzyme is added to a solution containing ATP and equal parts of glucose, fructose, and sucrose?

A. All of the glucose + fructose will be converted to sucrose.

B. All of the sucrose will be converted to glucose + sucrose.

C. The glucose + fructose will reach their equilibrium constant with sucrose.

D. The ATP will phosphorylate the glucose to produce sucrose while leaving fructose.

2.Which of the following does not contribute to how an individual protein functions?

A. sequence of amino acids.

B. The quaternary structure of that protein.

C. The shape of the binding site.

D. The number and position of charged and polar amino acids.

3. In order to perform functions that proteins alone cannot do, proteins can:

A. Incorporate other molecules into their structure.

B. bind to other proteins to form a complex.

C. signal to non-protein enzymes to perform the function.

D. undergo a conformational change to perform the function.

4. Which of the following is not a function of intrinsically disordered sequences in a protein?

A. Acting as substrates for chemical interactions.

B. Increasing variation in a protein by swapping amino acids.

C. Providing elasticity to tissues.

D. Flexing to enable interactions between domains.

1. A polypeptide chain has a large percentage of acidic and basic amino acids in it. The R groups of these amino acids form ionic interactions, which helps the protein to maintain it’s structure. This particular polypeptide works well under an optimum pH of 7. Ignoring effects of strong acids and bases on peptide bonds, what will happen to the tertiary structure of the protein if you move it stomach acid, which has a pH of 1-2. Why? Be specific regarding what influence the pH will have on the bonds maintaining tertiary structure in the molecule. Include the amino acid charges of the acidic and basic amino acids at the acidic pH, as well as the concept of pK in your answer. Assume that acidic amino acids have a pK of approximately 4.7 and basic amino acids have a pK of approximately 10.

2. Ignoring peptide length (or lack thereof) where would this portion of a polypeptide be most likely to be found: On the inside or on the outside surface of a protein floating around in the cytoplasm? Explain

3. A mutation occurs in the SRC kinase such that the tyrosine on the loop over the active site is changed to aspartic acid. This mutation mimics phosphorylation.
a. knowing what you know about the properties of phosphate groups and aspartic acid, why does aspartic acid mimic phosphorylation?
b. What would be the implication of this mutation on the function of the SRC kinase?

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