1. Given the following amino acids, explain where they would be found in the tertiary structure of a protein and WHY (lack of explanation/incorrect explanations will NOT receive full credit; assume living system of pH = 7.4).
Arg Phe Pro Glu His
Ala Tyr Val Cys
Arginine: This is a charged amino acid that is extremely hydrophilic. It is hydrophilic because while it has an aliphatic side chain that is hydrophobic, it also has two groups where a positive charge resonates between the two making the molecule very hydrophilic. Therefore, it would be found in the outer area of the proteins 3D structure because it would want to interact with water.
Phenylalanine: This amino acid would be found in the interior near the protein core where …show more content…
By losing their structure, this means losing either their secondary, tertiary, or quaternary structure. A way that proteins denature is when the environment that they are in changes, that is, the pH changes. When a pH change occurs in solution, molecules are likely to undergo an ionic change where side chains can gain or lose a proton. This means some side chains could gain a proton, or lose a proton, either way it could ultimately change how the protein is folded (Holme, 2016). Another way that a protein can denature is by adding heat (temperature) to the protein. The mechanism behind this looks at the hydrogen bonds that are present in secondary, tertiary and quaternary structures. Hydrogen bonds are known as non-covalent bonds and are very weak bonds, meaning that they can be disrupted very easily. When heat is added to a protein, their hydrogen bonds can easily get disturbed and cause them to break off of the protein. This can create somewhat of a chain reaction because when a hydrogen breaks off a molecule, it makes it easier for another hydrogen to break off. Another way that a protein can denature is by adding the protein to alcohol. Alcohol is a very strong substance and has the ability to disrupt the hydrogen bonding that the protein has and create new bonding. The new bonding consists of the alcohol forming bonds with the proteins side chains, therefore, denaturing the protein (Ophardt,
Arg Phe Pro Glu His
Ala Tyr Val Cys
Arginine: This is a charged amino acid that is extremely hydrophilic. It is hydrophilic because while it has an aliphatic side chain that is hydrophobic, it also has two groups where a positive charge resonates between the two making the molecule very hydrophilic. Therefore, it would be found in the outer area of the proteins 3D structure because it would want to interact with water.
Phenylalanine: This amino acid would be found in the interior near the protein core where …show more content…
By losing their structure, this means losing either their secondary, tertiary, or quaternary structure. A way that proteins denature is when the environment that they are in changes, that is, the pH changes. When a pH change occurs in solution, molecules are likely to undergo an ionic change where side chains can gain or lose a proton. This means some side chains could gain a proton, or lose a proton, either way it could ultimately change how the protein is folded (Holme, 2016). Another way that a protein can denature is by adding heat (temperature) to the protein. The mechanism behind this looks at the hydrogen bonds that are present in secondary, tertiary and quaternary structures. Hydrogen bonds are known as non-covalent bonds and are very weak bonds, meaning that they can be disrupted very easily. When heat is added to a protein, their hydrogen bonds can easily get disturbed and cause them to break off of the protein. This can create somewhat of a chain reaction because when a hydrogen breaks off a molecule, it makes it easier for another hydrogen to break off. Another way that a protein can denature is by adding the protein to alcohol. Alcohol is a very strong substance and has the ability to disrupt the hydrogen bonding that the protein has and create new bonding. The new bonding consists of the alcohol forming bonds with the proteins side chains, therefore, denaturing the protein (Ophardt,