20-Bio-A3 Biomechanics · December 2018
Nivaar worked solution (AI-drafted; not reviewed by a licensed engineer)
National Exams — December 2018 — 04-Bio-A3, Cellular and Molecular Biology and Biochemistry. Three-hour, CLOSED-BOOK exam; only an approved Casio or Sharp calculator is permitted. The paper carries six questions of equal value (20 marks each): FIVE questions constitute a complete paper and only the first five as they appear in the answer book are marked (100 marks total), with candidates urged to state any interpretive assumptions in writing. All SIX questions are worked below as a complete study resource. Question 6 is a 20-item True/False set marked +1 for a correct answer, 0 for a blank, and −1 for an incorrect answer.
Reference texts: Alberts et al., Molecular Biology of the Cell (6th ed.) — cell structure, gene regulation, DNA/RNA/protein synthesis; Nelson & Cox, Lehninger Principles of Biochemistry (7th ed.) — enzyme kinetics, Michaelis–Menten and substrate inhibition; Sambrook & Russell, Molecular Cloning: A Laboratory Manual (4th ed.) — restriction mapping, Sanger sequencing; Murphy & Weaver, Janeway's Immunobiology (9th ed.) — antibody structure and function; Murray et al., Medical Microbiology (9th ed.) — antibiotic mechanisms and susceptibility testing.
Question text not reproduced: the examination questions are © Engineers and Geoscientists BC. Open the official past paper (linked at the top of this page) to read the question, then follow the worked solution below.
Approach. Each statement is evaluated against the precise underlying molecular/cell biology definition it tests; several items are deliberately constructed as a plausible-sounding but swapped, inverted, or mis-attributed version of a true fact and must be checked term-by-term rather than pattern-matched.
| # | Statement (paraphrased) | Verdict | Rationale |
|---|---|---|---|
| 1 | Hydrogen bonds are weak/broken by thermal energy, yet contribute significantly to the specificity of macromolecular interactions. | True | Individually weak and reversible, but numerous and highly directional (base pairing, protein folding) — their collective geometry, not individual strength, gives specificity. |
| 2 | The active site of an enzyme usually occupies only a small fraction of the enzyme surface. | True | Standard biochemistry — the catalytic pocket is a small, precisely shaped region of an otherwise much larger protein. |
| 3 | Non-covalent bonds are too weak to influence the 3D structure of macromolecules. | False | Non-covalent interactions (H-bonds, ionic, hydrophobic, van der Waals) collectively determine secondary, tertiary and quaternary structure. |
| 4 | Affinity chromatography separates molecules according to their intrinsic charge. | False | That describes ion-exchange chromatography; affinity chromatography separates based on a specific binding interaction (e.g. antibody–antigen, enzyme–ligand). |
| 5 | Proteins can carry overall negative, positive, or no charge depending on solution pH. | True | Amphoteric behaviour; net charge depends on pH relative to the protein's isoelectric point (pI). |
| 6 | Ultracentrifugation allows greater separation of small molecules than centrifugation at lower g-force. | True | Higher gravitational force is needed to resolve/sediment smaller particles with higher resolving power. |
| 7 | If 14% of a bacterial DNA's nucleotides are adenine, must 36% be guanine? | True | Chargaff's rules (dsDNA): %A=%T so %T=14%, leaving %G+%C=72%, and %G=%C so each is 36%. |
| 8 | A G–C base pair is stabilized by at most two hydrogen bonds. | False | G–C pairs form THREE hydrogen bonds; A–T pairs form two — the statement has the count backwards. |
| 9 | During interphase, DNA is in the nucleus and each chromosome can be easily identified without staining. | False | Interphase chromatin is decondensed/diffuse; individual chromosomes are not distinguishable without staining (or condensation, as in mitosis). |
| 10 | Two closely related species should have the same number of chromosomes. | False | Chromosome number varies widely even between closely related species due to chromosomal fusions/rearrangements; relatedness does not fix karyotype. |
| 11 | Chromosomes, chromatin and chromatids all refer to DNA in association with proteins. | True | All three terms describe DNA–histone/protein complexes at different packaging states (general complex, condensed structure, one replicated copy). |
| 12 | Chromatids are always present in the cell. | False | Sister chromatids exist only after DNA replication (S phase through mitosis); a G1 chromosome has a single chromatid. |
| 13 | DNA was shown to be the hereditary material by an experiment where live VIRUS took up DNA from lysed cells. | False | The classic transformation experiment (Avery, MacLeod & McCarty) used live BACTERIA taking up DNA released from lysed/heat-killed bacteria, not a virus. |
| 14 | Chemical modification of histones (e.g. methylation) can regulate DNA packing in eukaryotic chromosomes. | True | Epigenetic histone modifications (methylation, acetylation) directly regulate chromatin condensation state. |
| 15 | Ion-exchange chromatography separates molecules based on charge. | True | Correct definition of ion-exchange chromatography. |
| 16 | SDS-PAGE separates proteins based on charge. | False | SDS coats proteins with a uniform negative charge-to-mass ratio and denatures them, so separation is by molecular SIZE, not native charge. |
| 17 | Only the sulfur in cysteine residues can form disulfide bridges in proteins. | True | Disulfide bonds form between cysteine thiol (–SH) side chains specifically; methionine's thioether sulfur does not participate. |
| 18 | In gel-filtration chromatography, large molecules are recovered quicker because they cannot enter the porous material as easily as smaller molecules. | True | Correct description of size-exclusion chromatography — large molecules are excluded from pores and elute first. |
| 19 | A protein can have multiple functional domains. | True | Multidomain proteins (each domain often independently folded/functional) are common. |
| 20 | Antibodies and antibiotics are similar molecules that function in similar ways. | False | Antibodies are large immune-system glycoproteins that bind antigens specifically; antibiotics are structurally diverse small molecules acting through distinct microbial-target mechanisms (see Question 3). |