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In a given protein (Enzyme), amino acid Lysine is replaces by aspartic acid and amino acid glycine is replacedby cysteine. Does this change occur in the primary and or secondary. Explain how it might result in change in the tertiary protein structure. Do you think that there will be an effect of the enzyme action and/or activity? Explain.

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Reid Wolff
Reid WolffLv2
28 Sep 2019
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Related questions

Suppose that, in a given protein, one lysine is replaced by aspartic acid. Does this charge occur in the primary structure or in the secondary structure? How might it result in a change in tertiary structure? In quaternary structure? Would this be considered a mutation? In humans mutations can lead to a number of diseases or disorders, please list one and detail/ describe the mutation along with the disease/ disorder.

Assuming that the mutations are adaptive, how would that affect the stability of a protein at low and high temperatures?

Given:

1) Glutamine to lysine in a warm adapted species.Glutamine is uncharged while lysine is positively charged, therefore there would likely be a change as an uncharged amino acid is being replaced with positively charged amino acid.

2) Threonine to Alanine in a warm adapted species. Threonine is polar uncharged while Alanine is hydrophobictherefore there would likely be a change, as a polar charged amino acid is being replaced with a hydrophobic amino acid.

3) Glutamic acid to aspartic acid in a cold adapted species. Both Aspartic acid to Glutamic acid are negatively charged, therefore, there would likely be no effect with this change as both are negatively charged amino acids.

4) Glycine to alanine in a warm adapted species. Both Glycine to Alanine are non polar amino acids, therefore the change would likely have no effect as both are non polar and hydrophobic.

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 itҀ™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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