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CHEM120 Biochemsitry - Final Assessment Review - Mod 1 2025

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CHEM120 Biochemsitry - Final Assessment Review - Mod 1 2025CHEM120 Biochemsitry - Final Assessment Review - Mod 1 2025CHEM120 Biochemsitry - Final Assessment Review - Mod 1 2025CHEM120 Biochemsitry - Final Assessment Review - Mod 1 2025

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Institution
Portage Learning
Course
CHEM120

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CHEM210 Biochemistry

Final Assessment Review

Module 1 (Questions & Solutions)

2025




©2025

, 1. Case Study – Enzyme Kinetics and Inhibition:
A researcher examines the enzyme-catalyzed conversion of substrate X
into product Y. By charting a Michaelis–Menten curve, she observes that
after adding an inhibitor, the apparent Km increases while the Vmax
remains unchanged.
Question: Which type of inhibition does this study most likely
demonstrate?
A. Noncompetitive inhibition
B. Uncompetitive inhibition
C. Competitive inhibition
D. Mixed inhibition

ANS: C. Competitive inhibition
Rationale: Competitive inhibitors bind to the enzyme’s active site,
competing with the substrate. This increases the measured Km
(indicating lower affinity) without affecting Vmax, as higher substrate
concentrations can overcome the inhibition.

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2. Case Study – Protein Folding and Misfolding:
In a laboratory investigation of protein X, researchers observe that a
point mutation disrupts the hydrophobic core, causing misfolding and
amyloid aggregation.
Question: Which cellular mechanism is most directly affected by this
mutation?
A. Transcriptional regulation
B. Chaperone‑mediated folding
C. Posttranslational glycosylation
D. mRNA splicing

ANS: B. Chaperone‑mediated folding
©2025

, Rationale: Molecular chaperones assist in the correct folding of
proteins. A point mutation that disrupts the hydrophobic interactions can
overwhelm chaperone systems, leading to misfolding and aggregation.

---

3. Case Study – Carbohydrate Structure:
A scientist isolates a complex plant polysaccharide and finds that its
monomer units are linked by glycosidic bonds between the anomeric
carbon of one sugar and a hydroxyl group of another.
Question: Which structural feature is commonly associated with these
glycosidic linkages?
A. Peptide bond formation
B. Phosphodiester linkage
C. Formation of either α- or β-anomers
D. Disulfide bond formation

ANS: C. Formation of either α- or β-anomers
Rationale: During glycosidic bond formation, the configuration at the
anomeric carbon (α or β) is critical. These anomers affect the three-
dimensional structure and properties of the polysaccharide.

---

4. Case Study – Lipid Bilayer Dynamics:
In a study of membrane fluidity, a researcher increases the temperature
of a phospholipid bilayer and notes an increased lateral movement of
lipid molecules.
Question: Which statement best describes the effect of temperature
on membrane fluidity?
A. Higher temperatures decrease fluidity by increasing hydrogen bond
strength.
B. Higher temperatures increase fluidity by reducing van der Waals
interactions among fatty acid chains.
C. Lower temperatures increase fluidity because of enhanced rotational
©2025

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