Question

A. If the original amino acid was responsible for the tertiary structure of the protein, what type of interaction was most likely involved? Explain how you chose your answer, using terms we have discussed in lecture or the text for this class.

B. Instead of the replacement amino acid listed to the right of the arrow below, what amino acid might replace the original and have an even worse effect on the protein? Explain how you chose your answer, using terms we have discussed in lecture or the text for this class. Your explanation should compare the similarities and/or differences between the original and the replacement listed below, plus your proposed answer.

C. Instead of the replacement amino acid listed to the right of the arrow below, what amino acid might replace the original and have a less effect on the protein? Explain how you chose your answer, using terms we have discussed in lecture or the text for this class. Your explanation should compare the similarities and/or differences between the original and the replacement listed below, plus your proposed answer.

Answer 1

Hydrophobic interaction is the most likely type of interaction involved in maintaining the tertiary structure of a protein. If the replacement amino acid has a more hydrophilic or polar side chain, it could have an even worse effect on the protein. However, if the replacement amino acid has a similar hydrophobic side chain, it may have a less effect on the protein.

Step-by-step explanation:

The type of interaction that is most likely involved in maintaining the tertiary structure of a protein is hydrophobic interaction. Hydrophobic interactions occur between nonpolar side chains of amino acids, which can form a stable core in the protein's three-dimensional structure. This interaction is driven by the tendency of nonpolar side chains to minimize contact with water.

If the replacement amino acid has a more hydrophilic or polar side chain, it could disrupt the hydrophobic interaction and have an even worse effect on the protein. For example, if a hydrophobic amino acid is replaced by a hydrophilic amino acid such as glutamic acid, which has a negatively charged side chain, it would disrupt the hydrophobic core and potentially lead to protein misfolding or instability.

On the other hand, if the replacement amino acid has a similar hydrophobic side chain, it may have a less effect on the protein. For example, if a hydrophobic amino acid with a nonpolar side chain is replaced by another hydrophobic amino acid with a similar nonpolar side chain, the overall hydrophobic interaction in the protein may be maintained, leading to less disruption in the tertiary structure.