Bio Discussion 1 Severe Fever

When you have a severe fever, what may be a grave consequence if this is not controlled? A. destruction of your enzymes' primary structure B. removal of amine groups from your proteins C. change in the folding of enzymes D. removal of the amino acids in active sites E. binding of enzymes to inappropriate substrates The shape of an enzyme is critical to its function; enzymes have specific shapes which determine the substrates that can bind to their active sites. Most enzymes are proteins, and they must exist in certain conditions in order to survive and/or function properly. One such factor that enzymes depend on is temperature, and when temperatures get too high enzymes go through denaturalization. Denaturation is when the proteins are exposed to extreme heat and as a result, begin to unfold and lose their very important shape (Citovsky, Lect. 4). When a person gets a fever, the body will increase in temperature, and this increase results in denaturation of proteins that function as enzymes. Answer A. Destruction of your enzymes’ primary structure is incorrect. Denaturation affects all structures of proteins except primary structure, so that is why this cannot be the answer (Citovsky, Lect. 4). The primary structure of a protein is its amino acid sequence which is the composition of the polypeptide chain. This polypeptide chain keeps its amino acids attached with peptide bonds between the carboxyl and amino group of adjacent amino acids; the process of creating the peptide bond is dehydration synthesis, where water is created through the loss of hydrogen and oxygen atoms (Citovsky, Lect. 3). Severe heat will not disrupt this aspect of proteins. Answer B. Removal of amine groups from your proteins is incorrect. An amine group is a part of each amino acid that makes up a protein. In addition to that group, each amino group also contains a carboxyl group, a central carbon, and a unique side chain (Citovsky, Lect. 3). The amine groups are bonded to the carboxyl groups through peptide bonds in the primary structure of a protein, and therefore they are not disrupted by a temperature change and cannot be removed from each individual amino acid. Answer D. Removal of the amino acids in active sites is incorrect. The active site of an enzyme is where the substrate binds to the enzyme and thus where the enzyme can help break apart of form a bond in order to speed up a reaction (Citovsky, Lect. 4). To remove amino acids from a protein, in this case an enzyme’s active site, would involve disrupting its primary structure (primary structure is the sequence of amino acids), and a rise in temperature cannot cause this, even if it could cause denaturation. Answer E. Binding of enzymes to inappropriate substrates is incorrect. When an enzyme denatures due to a fever, it loses its shape completely and reverts back to its primary structure, simply a polypeptide chain. There would be no active site in existence any longer for an enzyme to bind to any substrate, let alone an inappropriate one. Answer C. Change in the folding of enzymes is the correct answer. Because a severe enough fever will cause denaturation of proteins, their structures will unwind, specifically their secondary, tertiary, and quaternary structures. Secondary structure is the alpha helices and beta pleated sheets formed by the bonds in the backbone of the polypeptide chain, while tertiary structure is based on the folding of the chain based on different bonds formed by the side chains on each amino acid, some being hydrophobic, hydrogen, disulfide, and ionic (Citovsky, Lect. 3). Quaternary structure is when multiple protein subunits come together to make a single unit, like hemoglobin for example (Citovsky, Lect. 4). When proteins denature, these structures are disrupted and the bonds in alpha helices and beta pleated sheets, side chains, and larger protein subunits will break and therefore the protein itself will unfold, which is why answer C is the correct answer choice. In modern day science applications, scientists are taking advantage of every type of biological process, even those which may seem unhelpful such as the process of denaturation. One such way in which denaturation is being used in the scientific world is to help stop the spread of the hepatitis A virus. A common way that it is spread is through uncleaned berries, but recent research has shown that when the berries are cleaned in a solution of heat-denatured lysozyme, it kills the HAV (Takahashi, pg 104).