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WGU C785 Final Exam 2024 With All The Correct Answers

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WGU C785 Final Exam 2024 With All The Correct Answers

Institution
BioChem C785
Course
BioChem C785










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Institution
BioChem C785
Course
BioChem C785

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Uploaded on
October 10, 2025
Number of pages
27
Written in
2025/2026
Type
Exam (elaborations)
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WGU C785 FINAL EXAM 2024 WITH ALL THE CORRECT
ANSWERS



1. What is the basic structure of an amino acid? What do they look like?:
ANS>> amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and
variable group
2. How do you identify the 3 different types of side chains:
ANS>> non-polar/hydropho- bic, polar, and charged?: Non-polar/hydrophobic - end
with CH or "can't have" water. Polar - end with OH, SH, or NH. Charged - end with a charge
3. what kinds of bonds do each of the 3 different types of side chains
make?:
ANS>> ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure?:
ANS>> Primary - linear structure, Secondary - Folded into helix or pleated sheet caused
by hydrogen bonding, tertiary - 3D structure caused by side chain interactions, quaternary
- 1+ amino acid chains combine = multiple subunits MUST have 1+ subunit
5. What enviormental change breaks each type of bond?:
ANS>> hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen -
temperature, change in pH, disulfide - reducing agents
6. what type of amino acid side chain leads to protein aggregration?:
ANS>> hydrophobic bonds
7. how do environmental changes affect protein folding?:
ANS>> Extreme temp can cause hydro- gen bonds to break apart = malformation of
protein folding
8. how do mutations affect protein structure?:
ANS>> Can cause structure to change. Protein loses form
= loses function. May form a ditterent protein.
9. What is an electron?:
ANS>> Negatively charged atom on outer ring for bonding
10. What is energy::
ANS>> Power derived fro chemical interaction
11. what are covalent bonds?:


,WGU C785 FINAL EXAM 2024 WITH ALL THE CORRECT
ANSWERS


ANS>> chemical bond, atoms share 1+ valence electrons
12. what is an ionic bond?:
ANS>> bond between positive and negative
13. what is a hydrogen bond?:
ANS>> weak bond between positive and negative
14. with an amino?:
ANS>> piece of amino acid, NH2 or NH3
15. what is a carboyxl?:
ANS>> piece of amino acid, COO or COOH
16. What is hydrophobic?:
ANS>> Doesn't like water, end with CH
17. what is hydrophilic?:
ANS>> Water Lovering, end with OH, NH, or SH
18. what is disulfide bond?:
ANS>> strongest bond between reduction agents, formed between SH's.
19. what are zwitterions?:
ANS>> amino with positive and negative charges = overall charge of zero
20. what is a polypeptide:
ANS>> polymer of amino acids
21. What is dehydration synthesis?:
ANS>> Process of forming peptide bonds
22. what is hydrolysis?:
ANS>> adding water to destroy bonds






,WGU C785 FINAL EXAM 2024 WITH ALL THE CORRECT
ANSWERS



23. what is an alpha helix?:
ANS>> twisted secondary structure, formed by hydrogen bonds
24. what is a beta sheet?:
ANS>> folded second structure shape, formed by hydrogen bonds
25. what is denaturation?:
ANS>> loss of shape duet o interruption of chemical bonds; occurs via extreme salt,
temp, pH
26. what is aggregation?:
ANS>> clumping of inner or outer cellular proteins caused by misfolded proteins leading to
diseases such as Alzheimers, ALS, Parkinson's
27. how do enzymes catalyze reactions?:
ANS>> bind with substrates to decrease activation energy required and decrease
reaction rate
28. how do enzymes affect reaction rate and activation energy?:
ANS>> decrease activation energy and decrease reaction rate
29. what are the 4 steps of the enzymatic cycle?:
ANS>> enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released, enzyme recycled
30. how do environmental changes affect enzymes?:
ANS>> High heat, pH change, high salt concen- tration, and reducing agents can cause
an enzyme to lose its form/lose function
31. what is a competitive inhibitor?:
ANS>> Mimics substrate and takes its place on the active binding site
32. what is a noncompetitive inhibitor?:
ANS>> Binds to allosteric site causing active site to change shape = preventing
substrate from binding with enzyme
33. what molecules increase/build up or decrease given a specific
inhibitor? A
-> (enzyme 1) -> B -> (enzyme 2) -> C -> (enzyme 3) -> D. Pretend
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