8fc93bea-e7cb-4195-87c9-f3835becd068

AP Biology Name: ______________
Lesson 2 Week 3: Unit 1 Practice FRQ
Instructions:
1. Watch the video updates on the AP Exam, and how that will affect our class.
2. Watch Lesson 1 Week 3: Unit 1 Review video on classroom.
3. Complete the Unit 1 Review MCQ on college board.
4. Complete Lesson 2 Week 3: Unit 1 Practice FRQ below.
Directions: Read each question carefully. Write your response in the space provided for each part of each question.
Answers must be written out in paragraph form. Outlines, bulleted lists, or diagrams alone are not acceptable and
will not be scored.
Question 1. This question is worth 2 points.
The secondary compound cyanide (Figure 1) is a toxic, bitter-tasting chemical that is found in apple seeds. Cyanide
in seeds is only released and tasted if the seed is crushed. When animals eat apples, they typically eat the sweet
fleshy part of the fruit and spit out the seeds or swallow them whole.
Based on the chemical structure of cyanide, identify ONE type of biological macromolecule that could serve as a
chemical precursor for the production of cyanide in a plant. Justify your choice.
- Response:
One type of biological macromolecule that could serve as a chemical precursor for the production of cyanide in a
plant are nucleic acids, since new plants are grown from apple seeds, indicating that they contain genetic material,
which is only found in nucleic acids. Moreover, it mentions that cyanide tastes bitter, which means it has to be
more basic in pH, and nucleotides like RNA contain more hydroxide, which could hypothetically make them taste
bitter. Lastly, cyanide contains nitrogen, carbon, and hydrogen, which nucleic acids also contain.
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Question 2. This question is worth 1 point.
The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate concentrations in the
presence of a constant concentration of the enzyme.
Connect the primary structure of the enzyme to its overall shape.
- Response:
The primary structure of the enzyme connects to its overall shape because primary structure is related to
the linear sequence of amino acids. Changing the order of this sequence would change structure, which
would in turn change the shape, since the sequence helds determine how the polypeptide will fold in
secondary and tertiary structure, because of the interaction of R groups (the amino acid groups in the
sequence), which would change the 2D and 3D shapes.
Atherosclerosis is a disease that results when certain cells and proteins of an individual’s body adhere to and
damage blood vessels, especially those around the heart. Researchers continue to look for improved ways to treat
individuals with the disease. Data obtained from earlier experiments suggested that it might be possible to reduce
damage to the blood vessels by increasing the expression of FXR1, an RNA-binding protein in the muscle cells that
form the outer surface of the blood vessels. Additional data suggested that IL-19, a protein secreted by certain
white blood cells, might regulate expression of the FXR1 gene.
To investigate the regulation of the FXR1 gene by IL-19, a researcher added IL-19 to vessel-lining muscle cells
growing in the lab. The researcher measured the amount of FXR1 protein produced by the cells over a period of 48
hours in the presence of IL-19. The researcher then calculated the relative amount of FXR1 present at each time
point compared with the amount of FXR1 at Time 0, whenIL-19 was first added to the cells. Data from three
replicate experiments are shown in Table 1.
TABLE 1. RELATIVE AMOUNT OF FXR1 PRODUCED BY CELLS IN RESPONSE

TO IL-19
(a) Describe how amino acids are categorized by their chemical properties. Explain how a change in the amino acid
sequence of the FXR1 protein could decrease the ability of the protein to bind to RNA.
- Response:
Amino acids differ from each other based on their R groups, which ultimately affect their structure and
function. Amino acids can also be categorized by their composition of elements, their polarity, their
charge, and their shape. A change in the sequence of the FXR1 protein could decrease the ability of the
protein to bind to RNA because the primary, secondary, and tertiary structure of the protein will change.
The primary structure is what is directly affected by the change in the sequence, but secondary structure
will change because two-dimensional folding, based on the interaction of local R groups, will differ
because the order is different. As a result, tertiary structure will be altered because three dimensional
folding is also dependent upon interactions with R groups, specifically the ones that may have once been
distant but are now closer because of changes in secondary structure. As a result, the polypeptide
changes completely, so it won’t be able to behave normally or bind properly to the RNA.
(b) Construct an appropriately labeled graph that represents the data shown in Table 1. Determine whether there is
a statistical difference in the amount of FXR1 protein produced by the cells after 16 and 24 hours in the presence
of IL-19.
- Response:
Yes, there appears to be a statistical difference in the amount of FXR1 protein produced by the cells after
16 and 24 hours in the presence of IL-19, because the relative amount of FXR1 protein at 16 hours (3.1 +/-
0.8) is much greater than the relative amount of FXR1 protein at 24 hours (2.15 +/- 0.405).
(c) Based on the data for the 48-hour period, describe the effect of IL-19 on FXR1 gene expression.
- Response:
The longer the cell is exposed to IL-19, the less likely it is to genetically express FXR1, as the relative
amount of FXR1 protein decreases as the time in the presence of IL-19 increases, indicating that they are
inversely proportional.
(d) The researcher hypothesizes that the FXR1 gene codes for a protein that binds to mRNAs that encode some
of the proteins that damage arteries. Individuals with a particular mutation of the FXR1 gene tend to have high
levels of these proteins. Based on this information, predict how the FXR1 protein most likely interacts with the
mRNAs.
- Response:
Based on the given information, the FXR1 gene most likely binds to the active site of the mRNA as the
initial substrate of the reaction that results in the final product of the artery-damaging proteins.
Scientists studying transcription in yeast (Saccharomyces cerevisiae) created an experimental strain that produced a
modified RNApolymerase containing a single amino acid substitution. The scientists determined the maximum
elongation rate during transcription with and without the modified RNA polymerase enzyme (Figure 1).
The compound amanitin, which is commonly found in toxic mushrooms, is a specific RNA polymerase inhibitor.
Amanitin binds to the RNA polymerase active site and inhibits transcription. In a second experiment, the scientists
treated the wild-type and experimental strains of S. cerevisiae with a 40 μg/mL solution of amanitin and recorded
the maximum elongation rate of the mRNA (Figure 2). Error bars represent ±2SEx¯
(a) Describe the three structural components of an RNA nucleotide monomer. Explain the role of RNA polymerase
during transcription.
- Response:
The three structural components of an RNA nucleotide monomer are a nitrogenous base (either adenine,
guanine, cytosine, or uracil), a phosphate group, and a five carbon sugar (specifically ribose). The role of
RNA polymerase during transcription is to “build” RNA by adding nucleotides only to the 3’ side,
complimentary to the template strand of DNA, except it uses uracil instead of thymine. When it is finished,
it separates from the DNA process, which ends transcription.
(b) Identify the dependent variable in the experiments. Identify a control group missing from the second experiment.
Justify the need for this control group in the second experiment.
- Response:
The dependent variable in the experiments is the maximum elongation rate (nucleotides/second). The
control group missing from the second experiment is the wild and experimental strains not exposed to the
amanitin solution. This control group is needed in the second experiment to see how the two strains would
behave in the absence of the amanitin solution, to better understand the extent of amanitin’s influence.
(c) Describe the effect of amanitin on the maximum elongation rate for the wild-type and modified RNA
polymerases. Determine the ratio of the average maximum elongation rate for the modified RNA polymerase
compared to the wild strain RNA polymerase in Figure 1.
- Response:
The amanitin significantly reduced both of the elongation rates of the wild-type and modified RNA
polymerases (by inhibiting transcription) and the elongation rates of the wild-type RNA polymerases
decreased slightly more than that of the modified RNA polymerases. The ratio of the average maximum
elongation rate for the modified RNA polymerase compared to the wild strain RNA polymerase in Figure 1
is 3:12, which is equivalent to 1:4.
(d) State the null hypothesis for the experiment in Figure 1. Provide reasoning to justify the claim that the change in
the amino acid sequence in the modified RNA polymerase affected the shape of the active site on the enzyme.
- Response:
Null hypothesis: The amino acid sequence has no relation to the structure, function, or
rate of elongation of RNA polymerase.
The change in the amino acid sequence in the modified RNA polymerase affected the
shape of the active site on the enzyme because the elongation rate for the modified
polymerase in figure 1 was significantly less than that of the wild, unmodified strain of
RNA polymerase. If the active site was changed, then the substrates wouldn’t be able to
bind to the RNA polymerase, making it difficult to build the RNA strand from the
complementary DNA strand during transcription, accounting for the lower elongation rate.
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AP Biology Name: ______________

Lesson 2 Week 3: Unit 1 Practice FRQ

Question 1. This question is worth 2 points.

Connect the primary structure of the enzyme to its overall shape.

Question 3. This question is worth 8 points.

TABLE 1. RELATIVE AMOUNT OF FXR1 PRODUCED BY CELLS IN RESPONSE

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