The name of this assignment is called Packback:
Packback is a mandatory interactive social media program we will use in BCHE 341. Participation is a requirement for this course, and the Packback Questions platform will be used for online discussion about class topics. In order to receive points per week, you must answer 2 question written by classmates and give your opinion and shed detail insight with your responses on the questions being asked.
Answer the below two questions in your own words according to the above information in part 1:
Question 1 that needs to be answered for this assignment:
Do you think there is an evolutionary advantage to having different blood types?
In Biology and Anatomy we learned that there are several different blood types; A, B, AB, and O. These types are necessary information when completing blood transfusions and similar operations; transfusing a different blood type could cause the body to reject the transfused blood. But how did variations in blood types evolve and what is the benefit of having various types?
Source: https://www.redcrossblood.org/donate-blood/blood-types.html
Question 2 that needs to be answered for this assignment:
Gathering that we have learned about the different types of reversible inhibitors, such as competitive, uncompetitive and non-competitive; how are irreversible inhibitors different? And can you name some examples of this type of irreversible inhibitor?
Irreversible inhibitors are considered the most toxic and dangerous type of inhibition since they permanently inactivate the enzyme (Chemistry Libretexts, 2021). Whereas, a reversible inhibitor can dissociate from the enzyme, allowing it to continue to work and catalyze reactions once it detaches itself.
How does the interaction with the enzyme differ between these two types of inhibitions?
Meaning, what makes the irreversible inhibition create permanent damage on the enzyme?
Source: Enzyme Inhibition. (2021, November 4). https://chem.libretexts.org/@go/page/16024
Below is an example of how the final work should be laid out for the two questions above when writing your responses to the above questions:
First written response
One Sentence Statement: An amino acid with hydrogen and carbon atoms and the R group can get de protonated or protonated when pH changes, therefore experiencing different changes.
Response to Question one: Each amino acid has another group of atoms bonded to a carbon atom called the R group or the side chain. Amino acids are amphoteric because they can act like bases and acids (Lumen, n.d.). A change in pH has the dipolar amino acid responding differently. For instance, at low pH or in an acidic solution, the amino acid group remains protonated, meaning that both the carboxyl group and amino group remain with their protons. On the other hand, both the amino and carboxyl groups lose protons at high pH, deprotonating. R groups can be polar, meaning they are neither hydrophobic nor hydrophilic, and therefore they are not positively or negatively charged. In my opinion, an increase in pH leads to the R group being deprotonated first before the ammonium group, and a decrease in pH leads to the R group being protonated.
Second written response:
One sentence statement: Proteins have different structure levels such as primary, tertiary, secondary, and quaternary structures
Response to question two: In dehydration synthesis, a peptide bond is formed between one amino acid from the carboxyl group and one more from the amino group. A polypeptide refers to a chain of amino acids. The tertiary structure of proteins refers to the three-dimensional arrangements of polypeptides, and proteins need this arrangement to function properly (Lubrizol Life Science, 2019). In contrast, the secondary structure of proteins refers to the regular arrangement of amino acids remnants in a polypeptide chain. However, tertiary structures are more stable than secondary structures of proteins because the tertiary structures are formed by folding the secondary structures, which create reinforced chains compared to the secondary structures, which only consist of polypeptide chains from amino acids, which make initial folding. Generally, the tertiary structures combine a secondary structure, which explains the stability of the tertiary structure.
