CHE102 Final Exam
Final Exam Instructions
Download this document and type your answers directly below each question. Do not paste any structures taken directly from the internet. You can draw them and take s photo of them, or create them from Marvin. Drawn structures need to be signed. Marvin structures need your initials. Once complete, save the file with your last name in the file name of the document. Submit to the appropriate Assignment box as one document.
For the short answer questions where you are asked to explain, answer the question in complete sentences. Limit your answer to 3-5 sentences, unless stated otherwise. Answer questions in your own words to show good comprehension. If you must quote something, include that reference in your answer with a proper citation.

1. What are the functions of enzymes in living organisms? Explain the induced fit model of enzymes? How do they affect chemical reactions in terms of energy? (3 pts)
2. What is an isoenzyme? Explain how doctors use LDH to diagnose whether someone has had a heart attack? Explain how isoenzymes play a role in the diagnosis. (3 pts)
3. The terms allosteric site and non-competitive inhibition are closely related. Explain how non-competitive inhibitors use allosteric sites to control enzyme activity. (3 pts)
4. In your own words, explain the difference between a non-competitive inhibitor and a competitive inhibitor. Why are irreversible inhibitors generally considered toxic? (3 pts)
5. RNA vaccines work differently than vaccines in the past. Instead of virus antigens being injected into the bloodstream, mRNA is injected. Answer the following questions that relate to the biochemistry of how a mRNA vaccine works. Draw a diagram with comments, if you like. (3 pts)
a. What kind of molecule does the mRNA code for in a mRNA vaccine?
b. By what process is this molecule produced in the cell?
c. What becomes of the mRNA after it produces these molecules?
6. Explain the similarities and differences between waxes and triglycerides in terms of chemical properties and function in living organisms. (3 pts)

A B C D
Figure 1: Structures of organic molecules and their interactions. Two molecule pairs are shown. On the left are Molecules A, then B and on the right are Molecules C, then D.
7. Identify the molecules (A, B, C, and D) and describe the molecular interactions shown in Figure 1. Why are these interactions important? (3 pts)
8. In Figure 1 you can see an R attached to each structure. What does the R represent? Is it a specific element? If so, what is the name of that element? (3 pts)
9. Explain how the arrangement of molecules in Figure 1 would be different in RNA, including the change(s) in the R-group(s). (3 pts)
10. Describe the difference between Translation and Transcription and where they occur. (3 pts)

11. Determine the genetic codes for the following sequence of 3 amino acids: Asn-Glu-Lys. (3 pts)
a. Provide one possible mRNA sequence for this peptide segment.
b. Provide the corresponding tRNA anticodon for each amino acid.
c. Provide the template DNA sequence for that mRNA.
Table 1: Table of codons for amino acids.

*START codon signals the initiation of a peptide chain.
*STOP codons signal the end of a peptide chain.

Figure 2: Biochemical pathway showing reactions between molecular structures and their enzymes.
Answer the following questions regarding the above pathway.
12. What are 3 names given for this pathway in Figure 2 and explain the reasoning for each name. (3 pts)
13. Identify which compounds in Figure 2 (if any) contain the following functional groups. Consider only the compounds framed in blue rectangles. (3 pts)
⦁ Amide
⦁ Alkene
⦁ Ketone
⦁ Alcohol
⦁ Ester

14. Identify which compound(s) in Figure 2 have chiral carbons. Identify any compounds that may have more than one chiral carbon. Consider only the compounds framed in blue rectangles. (3 pts)
15. Identify which compound(s) in Figure 2 have cis and trans isomers. Consider only the compounds framed in blue rectangles. (3 pts)
16. Draw the reaction that shows how oxaloacetate (shown in Figure 2) is made from the amino acid aspartate and α-ketoglutarate (shown in Figure 2)? Insert the drawing into this document. (3 pts)
17. Is aspartate an essential amino acid? Explain your answer. (3 pts)
18. The complete oxidation of glucose can produce 32 molecules of ATP. Glycolysis results in 7 of the 32 ATP molecules and the citric acid cycle results in 20 of the 32 ATP molecules. Explain where and how the remaining 5 molecules of ATP are produced from the complete oxidation of glucose. (3 pts)
19. Explain the difference between transamination and oxidative deamination. Which process contributes to the urea cycle? (3 pts)
20. Efficiency of ATP Production
The complete biological oxidation of one mole of glucose in cells normally produces about 32 moles of ATP. Each mole of ATP results in only about 7.3 kcal/mole ATP being stored as chemical energy to be used throughout the cell. Complete combustion of glucose in a calorimeter produces about 690 kcal/mole glucose. The biological oxidation turns out to be only about 33-34% efficient. The remaining energy in cells is lost as heat.
a. How much stored chemical energy in kcal is produced by the complete biological oxidation of one mole of glucose?
b.How much energy in kcal is stored in ATP from the complete biological oxidation of 30g of glucose if glucose has a molar mass of 180.2 g/mol?
c. How much heat is given off in kcal when 30g of glucose undergoes complete complete biological oxidation?