AP Biology Unit 1 Practice Questions: Chemistry of Life
10 original exam-style questions on Chemistry of Life. No account needed.
A student adds a competitive inhibitor to a series of enzyme reactions. In experiment 1, the inhibitor concentration is held constant while substrate concentration is varied. In experiment 2, the substrate concentration is held constant while inhibitor concentration is varied. The enzyme catalyzes the conversion of substrate S to product P.
Experiment 1: At low substrate concentrations, the reaction rate is significantly reduced compared to uninhibited controls. At very high substrate concentrations, the reaction rate approaches the uninhibited maximum (). Experiment 2: As inhibitor concentration increases, the apparent increases while remains unchanged.
- A would be unchanged and apparent would increase
- B would increase because the allosteric site enhances enzyme activity
- CBoth and would increase proportionally
- D would decrease and apparent would remain unchanged
Show answer and explanation
Correct answer: D
A noncompetitive inhibitor binds the allosteric site and reduces enzyme activity regardless of substrate concentration, decreasing without affecting substrate binding affinity (). Choice A describes the pattern for a competitive inhibitor, not a noncompetitive one.- AEnzyme activity increases because the hydrophobic residue forms stronger bonds with the substrate
- BEnzyme activity is unaffected because one amino acid change cannot alter tertiary structure
- CEnzyme activity decreases because the altered active site can no longer properly orient or bind the substrate
- DEnzyme activity increases because the loss of charge reduces product inhibition
Show answer and explanation
Correct answer: C
Active site residues are precisely positioned to bind substrate and facilitate catalysis; changing the charge of one active site residue can disrupt electrostatic interactions critical for substrate binding and transition state stabilization. Choice B is incorrect because active site residues are especially sensitive to amino acid changes.A student measures the activity of the enzyme amylase at various pH levels, keeping temperature and substrate concentration constant. The results are recorded in the table below.
| pH | Reaction Rate (mg starch/min) | Relative Activity (%) |
|---|---|---|
| 2 | 0.3 | 4 |
| 4 | 2.1 | 28 |
| 6 | 7.5 | 100 |
| 7 | 7.3 | 97 |
| 8 | 4.8 | 64 |
| 10 | 0.8 | 11 |
| 12 | 0.1 | 1 |
- AReaction rate increases because the inhibitor provides an alternate reaction pathway
- BThe optimal pH shifts to a higher value because the inhibitor changes enzyme conformation
- CReaction rate decreases permanently and cannot be restored by adding more substrate
- DReaction rate decreases but can be restored by adding more substrate
Show answer and explanation
Correct answer: D
A competitive inhibitor occupies the active site reversibly; increasing substrate concentration outcompetes the inhibitor for active site binding, restoring activity. Choice C describes irreversible (non-competitive) inhibition, not competitive inhibition.A student investigates the effect of pH on the activity of salivary amylase, an enzyme that hydrolyzes starch into maltose. She prepares identical starch-buffer solutions at varying pH values and adds equal amounts of enzyme extract. After 10 minutes at 37°C, she measures remaining starch concentration using iodine absorbance and calculates relative enzyme activity.
| pH | Remaining Starch (mg/mL) | Relative Activity (%) |
|---|---|---|
| 3.0 | 9.8 | 2 |
| 5.0 | 7.1 | 29 |
| 6.5 | 1.2 | 88 |
| 7.0 | 0.9 | 100 |
| 8.0 | 2.4 | 76 |
| 9.0 | 6.3 | 37 |
| 11.0 | 9.6 | 4 |
- AAt low pH, the substrate starch is hydrolyzed non-enzymatically, leaving less starch for the enzyme to act on
- BExcess hydrogen ions alter the ionization state of amino acid residues in the active site, disrupting the enzyme-substrate interaction
- CLow pH causes the starch molecules to polymerize into longer chains that cannot fit into the active site
- DAt acidic pH, the enzyme is degraded by other proteases present in the saliva sample
Show answer and explanation
Correct answer: B
Enzyme activity depends on the precise three-dimensional shape of the active site, which is maintained by weak interactions (hydrogen bonds, ionic bonds) involving ionizable amino acid side chains. At very low pH, excess H⁺ ions protonate these residues, altering their charge and disrupting the active site geometry so substrate binding fails. Choice A is incorrect because acid-catalyzed starch hydrolysis is negligible under these mild conditions and would not produce the observed pH-specific bell-shaped activity curve.- AStarch contains glucose monomers while cellulose contains fructose monomers
- BStarch is a lipid-protein complex while cellulose is a pure carbohydrate
- CCellulose contains more glucose monomers per chain, making it stronger but less soluble
- DThe glucose monomers in starch and cellulose differ in the type of glycosidic linkage: alpha in starch and beta in cellulose
Show answer and explanation
Correct answer: D
Starch has alpha-1,4-glycosidic bonds, producing a coiled, compact structure suitable for energy storage, while cellulose has beta-1,4-glycosidic bonds, producing straight chains that hydrogen-bond with neighboring chains for structural rigidity. The monomers in both are glucose (choice A is wrong).- AThe enzyme retains full activity because peptide bonds maintain the primary structure
- BThe enzyme is unaffected because hydrophobic interactions only stabilize the cell membrane, not proteins
- CThe enzyme activity increases because the unfolded protein has more surface area to bind substrate
- DThe enzyme activity decreases because tertiary structure is disrupted, altering the active site
Show answer and explanation
Correct answer: D
Hydrophobic interactions among nonpolar R-groups are critical stabilizers of tertiary structure; disrupting them causes the protein to unfold, distorting the active site geometry and reducing catalytic activity. Choice A is incorrect because primary structure alone does not confer enzymatic function.- ACarbohydrate; short-term energy storage accessible to cells during glycolysis
- BProtein; structural support of the extracellular matrix
- CLipid (triglyceride); long-term energy storage in adipose tissue
- DNucleic acid; storage of genetic information in the cell nucleus
Show answer and explanation
Correct answer: C
A glycerol backbone esterified to three fatty acids describes a triglyceride, the primary form of long-term energy storage in organisms. Triglycerides are hydrophobic (nonpolar) and yield more energy per gram than carbohydrates when catabolized.- AHydroxyl group ()
- BAmino group ()
- CCarboxyl group ()
- DPhosphate group ()
Show answer and explanation
Correct answer: C
The carboxyl group () donates a proton () at physiological pH, acting as an acid. The amino group () is actually basic, as it accepts protons, making choice B incorrect.- AAmino group ()
- BHydroxyl group ()
- CCarboxyl group ()
- DMethyl group ()
Show answer and explanation
Correct answer: C
The carboxyl group () donates a proton () in aqueous solution, making the solution more acidic; this is the defining property of organic acids like amino acids and fatty acids. Choice A is incorrect — the amino group acts as a base by accepting a proton, making solutions more basic, not more acidic.- AStarch is made of fructose monomers while cellulose is made of glucose, so different enzymes are required
- BStarch contains -glycosidic linkages that animal amylases can hydrolyze, while cellulose contains -1,4 glycosidic linkages that animal enzymes cannot break
- CCellulose is too large to enter cells, while starch can be broken down to small monomers small enough for absorption
- DStarch forms helical structures that facilitate enzyme binding, while cellulose forms linear chains that are inaccessible to digestive enzymes
Show answer and explanation
Correct answer: B
The critical difference is the linkage type: starch has -1,4 and -1,6 bonds that amylases cleave, while cellulose has -1,4 bonds that require cellulase enzymes absent in most animals. Choice D is partially true but not the primary explanation — the fundamental barrier is enzymatic specificity based on bond type, not physical accessibility.Want more than 10 questions?
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