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AP Biology

AP Bio Unit 3 MCQ Set B Data and Experiments

Shared by Ashton · Nov 12, 2026 · 0 plays

15 questions across 4 sections. After every answer you’ll see why each choice is right or wrong, not just the one you picked.

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Sample questions

Open a question to see the answer choices and the correct answer.

Based on the data, at about what pH does this amylase work best?
  1. A. pH 9
  2. B. pH 6
  3. C. pH 7 ✓
  4. D. pH 8

Correct answer: C. The highest rate (4.6 mg/min) is at pH 7.

By about what percentage does the rate decrease when pH changes from 7 to 9?
  1. A. About 410%
  2. B. About 3.7%
  3. C. About 80% ✓
  4. D. About 20%

Correct answer: C. (0.9 − 4.6) ÷ 4.6 × 100 ≈ −80%.

Which explanation best accounts for the low rate at pH 9?
  1. A. The starch is denatured at pH 9, so it can't enter the active site
  2. B. Fewer collisions happen because molecules move more slowly at high pH
  3. C. Disrupted R-group bonds change the active site's shape ✓
  4. D. Basic solutions supply hydroxide that acts as a competitive inhibitor

Correct answer: C. PH outside the optimum disrupts H-bonds and ionic interactions, changing the structure (3.2.A.1).

Which would be the most appropriate negative control for this experiment?
  1. A. Twice as much amylase in each pH buffer with the starch
  2. B. Starch in each pH buffer with no amylase added ✓
  3. C. Amylase and starch in water instead of buffer
  4. D. Amylase and starch at pH 7 only, since that's the optimum

Correct answer: B. It shows whether starch breaks down by itself at each pH, so the loss can be credited to amylase.

Which conclusion about Inhibitor Z is best supported by the data?
  1. A. It denatures the enzyme, since the rate at 1 mM drops by 65%
  2. B. It's noncompetitive: it lowers the rate at every substrate level
  3. C. It's an activator, because the rate increases with more substrate
  4. D. It's competitive: high substrate brings the rate close to normal ✓

Correct answer: D. At 20 mM, Z's rate (78) is close to the uninhibited rate (83). Extra substrate outcompetes it at the active site.