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Afe Babalola University

BCH 201: MEDICAL BIOCHEMISTRY I

Practice 402+ past questions for BCH 201 (MEDICAL BIOCHEMISTRY I) at Afe Babalola University. Organized by topic with explanations. Free preview on Testwiz.

402+ questions66 topics200 LevelTheory questionsTopic summaries
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About BCH 201 at Afe Babalola University

BCH 201 (Medical Biochemistry I) at Afe Babalola University (ABUAD) introduces students to the thermodynamic principles governing biological systems, including Gibbs free energy, reaction spontaneity, and bioenergetics. The course also covers enzyme kinetics and mechanisms such as the induced fit and lock and key models, enzyme classification, and inhibition, alongside essential topics in vitamin biochemistry (notably Vitamin A) and developmental anatomy, including fetal circulation and pharyngeal arch derivatives. This course is designed for undergraduate medical and health science students seeking a foundational understanding of how biochemical reactions drive physiological processes.

Practicing past questions by topic for BCH 201 helps students reinforce key concepts and identify recurring exam patterns. Topic-focused practice allows you to master difficult areas like enzyme inhibition or the differences between small and large intestines, improving retention and exam confidence. By targeting specific topics, you can efficiently allocate study time and build a solid grasp of both biochemical theory and its clinical applications, which is essential for success in ABUAD's medical biochemistry assessments.

Topics covered

Laws of Thermodynamics in Biological SystemsGibbs Free Energy and Reaction SpontaneityOpen vs Closed Systems in Living OrganismsBioenergetics and Energy TransductionInduced Fit Model of Enzyme ActionLock and Key Model of Enzyme ActionEnzyme Classification: OxidoreductasesExergonic and Endergonic ReactionsVitamin A Functions and RequirementsVitamin A DeficiencyFetal CirculationPharyngeal Arch Derivatives+54 more

Sample questions

1. Which of the following BEST describes the first law of thermodynamics as it applies to biological energy transductions?

a.Energy can be created but not destroyed in biological systems
b.Energy tends to become increasingly disordered in all natural processes
c.Energy may be changed from one form to another but cannot be created or destroyed
d.Energy transfer always results in an increase in the entropy of the universe

2. A biochemical reaction has a negative ΔG value. Which of the following conclusions is CORRECT?

a.The reaction is endothermic and absorbs heat from the surroundings
b.The reaction is endergonic and requires an input of energy
c.The reaction is exergonic and will proceed spontaneously
d.The reaction is at equilibrium and no net change occurs

3. Living organisms are classified as open systems because they:

a.Do not exchange either material or energy with their surroundings
b.Exchange energy but not material with their surroundings
c.Exchange both material and energy with their surroundings
d.Are always at equilibrium with their surroundings

4. Which of the following statements about the relationship between ΔG, ΔH, and ΔS is TRUE?

a.ΔG = ΔH - TΔS
b.ΔG = TΔS - ΔH
c.ΔG = ΔH × TΔS
d.ΔG = ΔH + TΔS

5. The oxidation of glucose by aerobic organisms results in an increase in the entropy of the surroundings because:

a.The organism itself undergoes a large increase in internal order
b.The free energy is converted into heat and entropy in the surroundings
c.The reaction results in a decrease in the number of molecules
d.The end products, CO₂ and H₂O, are returned to the surroundings

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Frequently asked questions

What is the difference between exergonic and endergonic reactions in biological systems?

Exergonic reactions release free energy (negative ΔG) and occur spontaneously, such as ATP hydrolysis. Endergonic reactions require an input of free energy (positive ΔG) and are non-spontaneous, such as protein synthesis. In living organisms, endergonic reactions are often coupled to exergonic reactions like ATP breakdown to drive essential processes.

How does the induced fit model differ from the lock and key model of enzyme action?

The lock and key model proposes that the enzyme's active site is rigid and perfectly complementary to the substrate, like a key fitting a lock. The induced fit model suggests that the active site is flexible and undergoes a conformational change upon substrate binding, which enhances catalysis. Most enzymes follow the induced fit model, as it better explains enzyme specificity and catalytic efficiency.

What are the main functions of Vitamin A and what happens in its deficiency?

Vitamin A (retinol) is essential for vision (as retinal in rhodopsin), immune function, cell growth, and epithelial tissue maintenance. Deficiency can cause night blindness, xerophthalmia (dry eyes), increased susceptibility to infections, and in severe cases, blindness. Adequate dietary intake from sources like liver, carrots, and leafy greens is necessary to prevent deficiency.

What are the key differences between the small and large intestine?

The small intestine is longer (about 6 meters), has villi and microvilli for absorption, and is the primary site for digestion and nutrient absorption. The large intestine is shorter (about 1.5 meters), lacks villi, and is mainly responsible for water and electrolyte absorption, and formation of feces. The small intestine has three parts (duodenum, jejunum, ileum), while the large intestine includes the cecum, colon, and rectum.

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