Instruction for Pack back Assignment 3

*Please read everything carefully before starting the assignment

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.

First thing to do for the assignment:

• When answering the two question above you must include the below a – c:

1. What is the thesis of your Response? Write a brief statement before your response to sum up what your response will discuss before you start writing the response.
2. Defend your Response. Make the case from your perspective on the topic of the question!! Why do you believe the argument you are making in your own response is correct or valid to what the classmate proposed in the questions? What data or examples can you include to support your perspective?
3. Cite your source by posting a link or typing a book title. Must have references for both questions and include at the bottom of the sheet.

• When writing the response of course give the facts and details on what you found through research, however, make it personal in the sense of write a written response for other class peers to read and understand where you are coming from on the topic of discussion. Let the peer know in your response whether you agree or disagree with the information they are providing us with in their description under their question.
• Please do not plagiarize any information found, put answers into your own words. Answer all parts of the two questions asked below fully and the professor said the answer needs to be strong answers with reasoning to back up why you feel the way you do about the subject. I will be graded on how strong the answer supports the questions.

Second thing to do for the assignment:

• Answer the below two questions in your own words according to the above information in part 1:

Question 1:

What makes induced fit an ideal model for most enzymes and their substrates?

In class we discussed that most enzymes utilize an induced fit relationship between the enzyme and an associated enzyme for accelerating a reaction. In this instance, the activation site can be induced by the substrate to complete a catalyzed reaction.

Why is this model more used than the lock and key model in enzyme activation?

Question 2:

Which enzyme inhibitors can be introduced to our body through food?

I found a very interesting article from Robert A. Burns, titled “Protease Inhibitors in Processed Plant Foods” which discusses the inhibition of serine protease. The article mentions how many legumes, such as soybeans, contain a protein inhibitor that affects trypsin and chymotrypsin when the food is not heated (Robert A. Burns, 1986). These inhibitors found in unheated legumes can affect the protein quality of the food, “induce pancreatic hypertrophy in some but not all experimental animals” and have been reported to be carcinogenic to the pancreas of laboratory rats (Robert A. Burns, 1986). Fortunately, the article describes that these levels of trypsin inhibition found in unheated legumes can be decreased by further processing the proteins.

Which other inhibitors can be introduced when eating? And how can we overcome such protein inhibitors?

• 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 Thesis 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 thesis 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.

References

Lubrizol Life Science. (2019, October 28). Protein structure: Primary, secondary, tertiary, Quatemary structures. LLS Health CDMO. https://lubrizolcdmo.com/technical-briefs/protein-structure/

Lumen. (n.d.). Peptide bonding between amino acids | Introduction to chemistry. Lumen Learning – Simple Book Production. https://courses.lumenlearning.com/introchem/chapter/peptide-bonding-between-amino-acids/