Unit 1: Biochemistry — Practice Quiz

Assessment AS Learning · Self-check · Strand B
Not Graded — Unlimited Retakes
Purpose: Self-assess your understanding of macromolecules, enzymes, and membrane transport. Each question has a worked solution.
Score: 0 / 12
Topic 1.1 — Macromolecules
Question 1
Which monomer pairs with which polymer correctly?
Solution: Glucose monomers join via alpha-1,4 (and alpha-1,6 branching) glycosidic bonds to form glycogen, the animal storage polysaccharide. Amino acids form proteins; nucleotides form nucleic acids; glycerol + 3 fatty acids form a triglyceride.
Question 2
A saturated fatty acid differs from an unsaturated fatty acid because it:
Solution: Saturated = no C=C; tails are straight, pack tightly, solid at room temperature (e.g., butter). Unsaturated has one or more C=C, creating kinks; usually liquid (oils).
Question 3
Which level of protein structure is stabilized primarily by hydrogen bonding between backbone atoms?
Solution: Secondary structure (alpha-helices, beta-sheets) is held by H-bonds between backbone N-H and C=O groups. Primary is the amino-acid sequence; tertiary involves R-group interactions (disulfide, ionic, hydrophobic); quaternary involves multiple subunits.
Topic 1.2 — Enzyme Kinetics
Question 4
In a Michaelis–Menten plot of reaction rate (v) vs [substrate], V_max represents:
Solution: V_max is the asymptotic maximum rate when every active site is occupied — adding more substrate cannot speed it up further. K_m = [S] at half V_max and is inversely related to enzyme–substrate affinity.
Question 5
A competitive inhibitor of an enzyme will:
Solution: A competitive inhibitor binds the active site, competing with substrate. With enough substrate, V_max can still be reached, so V_max is unchanged but apparent K_m rises (more substrate is needed for half V_max). Non-competitive inhibitors lower V_max.
Question 6
Calculate K_m: an enzyme reaches V_max = 80 µmol/min. At [S] = 5 mM, v = 40 µmol/min.
Solution: K_m = [S] at half V_max. Half V_max = 40 µmol/min, observed at [S] = 5 mM. Therefore K_m = 5 mM.
Question 7
The induced-fit model of enzyme action proposes that:
Solution: Koshland's induced-fit model: the active site is flexible. Substrate binding induces a conformational change that strains substrate bonds, lowering activation energy. Replaces the older rigid lock-and-key view.
Topic 1.3 — Cell Membrane & Transport
Question 8
Which transport mechanism requires ATP and moves a solute against its gradient?
Solution: Primary active transport (e.g., Na+/K+ ATPase: 3 Na+ out, 2 K+ in per ATP) hydrolyzes ATP directly to move solutes uphill. Facilitated diffusion uses channel/carrier proteins but follows the gradient (no ATP).
Question 9
A red blood cell placed in a hypotonic solution will:
Solution: In a hypotonic solution (lower solute outside), water enters the cell by osmosis. Animal cells lack a cell wall, so they swell and may lyse (hemolysis). Plant cells become turgid because the wall resists.
Question 10
In the fluid-mosaic model, which feature most affects membrane fluidity at low temperatures?
Solution: Cholesterol is a fluidity buffer: at low T it prevents tails packing too tightly (maintains fluidity); at high T it restrains motion (prevents excess fluidity). Unsaturated fatty acids (kinks) increase fluidity; saturated decrease it.
Question 11
Calculate water potential. A plant cell has solute potential ψ_s = −0.7 MPa and pressure potential ψ_p = +0.4 MPa. What is ψ?
Solution: ψ = ψ_s + ψ_p = −0.7 + 0.4 = −0.3 MPa. Water moves from higher (less negative) ψ to lower ψ.
Question 12
Endocytosis differs from facilitated diffusion because endocytosis:
Solution: Endocytosis (phagocytosis = solids; pinocytosis = fluids; receptor-mediated = specific) engulfs material in membrane vesicles, requires ATP and cytoskeletal rearrangement. Facilitated diffusion is passive, single-molecule, channel/carrier-mediated.