The amino acids that changed between the three species are;
- Amino acid 151 transited from valine to isoleucine in a warm adapted species.
- Amino acid 201 translated from glycine to alanine in warm adapted species.
- Amino acid 201 morphed from glutamine to lysine in warm adapted species.
- Amino acid 201 translated from glutamic acid to aspartic acid in cold adapted species.
<h3>What were the changes in the chemical properties of the R-groups?</h3>
The changes in the chemical properties of the R-groups are given as:
- Both valine and isoleucine are nonpolar.
- Both glycine and alanine are nonpolar.
- Glutamine is an uncharged polar group and Lysine is a charged polar group.
- Both glutamic acid and aspartic acid are charged polar group.
<h3>How might the changes that you identified affect the protein’s structure?</h3>
In scenario 1 and 2, the modifications would have zero effect.
In scenario 3, the polar groups are detected on the surface of the protein, thus, it is correct to state that both glutamine and lysine are polar and the modifications will have zero effect.
With regards to scenario 4, the change will have no impact, given that both glutamic acid and aspartic acids are R groups that are negatively charged.
<h3>Assuming that the mutations are adaptive, how should the changes that you identified affect the stability of the protein at low and high temperatures?</h3>
These mutations are critical for protein's three-dimensional structure stability.
For example, due to the proteins from thermophilic creatures, they are able to live at high temperatures and survive at low temperatures.
This is because they frequently have a large network of salt bridges on their protein surface, which offers thermo-stability to these proteins and prevents denaturation owing to the high temperatures in the environment.
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