Fiveable
🧬AP Biology
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FRQ 1 – Interpreting and Evaluating Experimental Results (Long)
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Unit 1: Chemistry of Life
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Practice FRQ 1 of 20
1. Enzymatic browning in damaged fruits is a chemical process catalyzed by the enzyme polyphenol oxidase (PPO). In the presence of oxygen, PPO converts phenolic compounds into dark-colored quinones.
PPO is a metalloenzyme that requires copper ions in its active site to function. Researchers investigated the effect of a copper-chelating agent, EDTA, on the activity of PPO extracted from Red Delicious apples. They hypothesized that removing copper ions would inhibit the enzyme's activity.
The researchers prepared PPO extracts and treated them with increasing concentrations of EDTA (0 mM, 5 mM, and 10 mM). They then measured the relative rate of quinone formation in each treatment group compared to the control (Figure 1).
The researchers then investigated a genetically modified 'Non-Browning' apple variety. They sequenced the PPO gene in both the Red Delicious and Non-Browning varieties and measured the total amount of quinone produced by extracts from each variety after 10 minutes (Figure 2).
A. Describe how the structure of an enzyme's active site contributes to its specificity for a substrate.

Figure 1. PPO activity in apple extracts

Single-panel vertical bar graph (no gridlines), white background, black axes and labels.

Axes (exact specifications):
- X-axis label: "EDTA Concentration (mM)".
- X-axis numeric range: from 0 to 12 (continuous numeric axis).
- X-axis tick marks: every 1 mM (ticks at 0, 1, 2, ..., 12) with labeled major ticks only at 0, 5, 10 (labels: "0", "5", "10").
- Y-axis label: "Relative PPO Activity (%)".
- Y-axis numeric range: from 0 to 120.
- Y-axis tick marks: every 10% (ticks at 0, 10, 20, ..., 120) with all tick labels shown.
- Origin: (0, 0) is present and the "0" at the origin is labeled on both axes.
- Axis arrows: arrows on the positive ends of both axes (right end of x-axis, top end of y-axis).

Bar geometry (treat bars as piecewise-constant ‘curves’ defined by control points; all bar tops are perfectly horizontal):
- There are exactly three bars, centered at x = 0, x = 5, and x = 10.
- Each bar has identical width: 1.0 mM total width.
  * For the 0 mM bar: left edge x = -0.5, right edge x = +0.5.
  * For the 5 mM bar: left edge x = 4.5, right edge x = 5.5.
  * For the 10 mM bar: left edge x = 9.5, right edge x = 10.5.
- Bar fill: solid medium-gray (no gradient). Bar outlines: black, 1.5 pt.

Exact bar heights (top edges) and required control points (each bar described by 5+ points so the renderer cannot shift values):
1) Bar for 0 mM EDTA (control): height exactly 100%.
   Control points tracing the bar perimeter (closed shape):
   - (-0.5, 0) closed corner → (-0.5, 100) → (0, 100) → (0.5, 100) → (0.5, 0) → (-0.5, 0) (returns to start).
   Curve behavior: all segments are straight lines; the top segment from (-0.5, 100) to (0.5, 100) is perfectly horizontal.

2) Bar for 5 mM EDTA: height exactly 40%.
   Control points (closed shape):
   - (4.5, 0) closed corner → (4.5, 40) → (5, 40) → (5.5, 40) → (5.5, 0) → (4.5, 0).
   Curve behavior: all segments straight; top is perfectly horizontal at y = 40.

3) Bar for 10 mM EDTA: height exactly 10%.
   Control points (closed shape):
   - (9.5, 0) closed corner → (9.5, 10) → (10, 10) → (10.5, 10) → (10.5, 0) → (9.5, 0).
   Curve behavior: all segments straight; top is perfectly horizontal at y = 10.

Error bars (explicit endpoints; draw as thin black lines with horizontal caps):
- Error bars are centered at the bar centers (x = 0, 5, 10).
- Each error bar has a vertical line plus two caps (top and bottom cap widths are exactly 0.6 mM wide, i.e., cap extends ±0.3 mM from bar center).
- Because the original prompt provides ±SE but not numeric SE values, set SE exactly to 0 for all groups so error bars are present but have zero length (caps coincide with the mean). This preserves numerical accuracy rather than inventing values.
  * 0 mM: mean 100; error bar endpoints at y = 100 and y = 100. Caps from x = -0.3 to +0.3 at y = 100.
  * 5 mM: mean 40; error bar endpoints at y = 40 and y = 40. Caps from x = 4.7 to 5.3 at y = 40.
  * 10 mM: mean 10; error bar endpoints at y = 10 and y = 10. Caps from x = 9.7 to 10.3 at y = 10.

Additional text/format constraints:
- No chart title inside the plotting area.
- No legend.
- All text in a single sans-serif font.
- Keep plotting area margins so the tallest bar top at y=100 is clearly below the y=120 tick.
B.
i. Identify the dependent variable in the experiment shown in Figure 1.
ii. Justify why the researchers included the 0 mM EDTA treatment group in the experiment shown in Figure 1.
iii. Based on Figure 1, describe the effect of increasing EDTA concentration on PPO activity.

Figure 2. Quinone production in apple varieties

Single-panel vertical bar graph (no gridlines), white background, black axes and labels.

Axes (exact specifications):
- X-axis label: "Apple Variety" (categorical shown on a numeric axis to force precise placement).
- X-axis numeric range: from 0 to 3.
- X-axis tick marks: every 0.5 (ticks at 0, 0.5, 1.0, 1.5, 2.0, 2.5, 3.0).
- X-axis category label placement (exact):
  * "Red Delicious" centered at x = 1.0.
  * "Non-Browning" centered at x = 2.0.
  Only these two category names are printed; other numeric tick labels may be present but should be visually deemphasized (lighter) if shown.
- Y-axis label: "Quinone Produced (µmol)".
- Y-axis numeric range: from 0 to 60.
- Y-axis tick marks: every 5 µmol (ticks at 0, 5, 10, ..., 60) with all tick labels shown.
- Origin: (0, 0) is present and the "0" at the origin is labeled on both axes.
- Axis arrows: arrows on the positive ends of both axes.

Bar geometry (bars are closed polygons; bar tops perfectly horizontal):
- Exactly two bars with identical width: 0.6 x-units total width.
  * Red Delicious bar: centered at x = 1.0, left edge x = 0.7, right edge x = 1.3.
  * Non-Browning bar: centered at x = 2.0, left edge x = 1.7, right edge x = 2.3.
- Bar fill: solid medium-gray; outline black, 1.5 pt.

Exact bar heights and control points (5+ per bar):
1) Red Delicious: height exactly 50 µmol.
   Control points (closed shape):
   - (0.7, 0) closed corner → (0.7, 50) → (1.0, 50) → (1.3, 50) → (1.3, 0) → (0.7, 0).
   Curve behavior: all segments straight; top segment is perfectly horizontal at y = 50.

2) Non-Browning: height exactly 2 µmol.
   Control points (closed shape):
   - (1.7, 0) closed corner → (1.7, 2) → (2.0, 2) → (2.3, 2) → (2.3, 0) → (1.7, 0).
   Curve behavior: all segments straight; top segment is perfectly horizontal at y = 2.

Error bars (explicit endpoints; do not invent SE magnitude):
- Error bars centered at x = 1.0 and x = 2.0.
- Cap width: exactly 0.4 x-units total (±0.2 from center).
- Set SE exactly to 0 for both groups (error bars present with zero length) because no SE values are provided.
  * Red Delicious: endpoints y = 50 and y = 50; caps from x = 0.8 to 1.2 at y = 50.
  * Non-Browning: endpoints y = 2 and y = 2; caps from x = 1.8 to 2.2 at y = 2.

Additional text/format constraints:
- No internal title.
- No legend.
- All text sans-serif, consistent size.
- Ensure the 2 µmol bar is clearly visible above the baseline (do not allow it to merge with the x-axis line).
C.
i. Identify the independent variable in the researchers' second experiment (data shown in Figure 2).
ii. Based on Figure 2, identify the apple variety that exhibits the lowest rate of enzymatic browning.
iii. The PPO gene in Red Delicious apples contains 1,725 coding nucleotides. In the Non-Browning variety, a mutation results in a coding sequence of only 450 nucleotides. Assuming all nucleotides in the coding sequences encode amino acids, calculate the difference in the number of amino acids between the functional PPO protein and the mutant protein.
D.
i. Researchers claim that the mutation in the Non-Browning variety renders the PPO enzyme non-functional. Using data from Figure 2, support the researchers' claim.
ii. Justify the claim that the truncated protein sequence in the Non-Browning variety results in a loss of enzyme function based on your understanding of protein structure.






Pep