AQA AS Level Biology Paper 1, November 2021: Question 5
8 marks · Medium difficulty · Short Answer
Describe how the structure of glycogen relates to its function, name the type of peptidase hydrolysing bond G, find the number of different R groups, and calculate the number of polypeptides of specific lengths from a digestion table.
Practise this questionQuestion
Question text
05.1 Describe how the structure of glycogen is related to its function.
[4 marks]
Figure 5 shows the primary structure of part of a polypeptide. Each shape
represents an amino acid. Identical amino acids have the same shape.
Figure 5
05.2 Name the type of peptidase which will hydrolyse the bond labelled G in Figure 5.
[1 mark]
05.3 Give the number of different R groups in the polypeptide shown in Figure 5.
[1 mark]
A scientist used an enzyme to digest a polypeptide containing 101 amino acids.
The digestion produced a range of smaller polypeptides.
The scientist determined the number of amino acids in each of the polypeptides
*10* produced. He also counted the number of polypeptides of each length.
Table 1 shows some of the scientist’s results.
Table 1
Number of amino acids in Number of polypeptides of each
polypeptide length
15 3
05.4 Use the information in Table 1 to calculate the number of polypeptides:
[2 marks]
6 amino acids in length
20 amino acids in length
Mark scheme
Show the mark scheme
Question Marking Guidance Mark Comments
05.1 1. Helix/coiled/branched so compact; 1. Accept description of
‘compact’, eg many
2. Polymer of glucose so easily hydrolysed; glucoses packed
closely/densely/tightly
3. Branched so more ends for faster hydrolysis;
4. Glucose (polymer) so provides respiratory
substrate for energy (release); 4 max
5. Insoluble so not (easily) lost (from cell)
OR
Insoluble so does not affect water
potential/osmosis;
05.2 Endo(peptidase); 1 Correct spelling
05.3 3; 1
1. (6 amino acids in length) 1;
05.4
Accept for 1 mark,
2. (20 amino acids in length) 2; 55 (2 5 + 3 15) if no
2 other mark awarded.
TOTAL 8
How to answer it
Biological Molecules & Enzymes Study Guide
What this question tests
This exam question evaluates your core knowledge of carbohydrate structure-function relationships (glycogen), protein primary structure interpretation, enzyme specificity (endopeptidases vs. exopeptidases), and quantitative data analysis involving peptide hydrolysis and molecular calculations.
Describe how the structure of glycogen is related to its function.
✅ Correct Answer / Mark Scheme
- Compact / Branched / Coiled: Fits a large amount of glucose into a small cellular space.
- Polymer of alpha-glucose: Easily hydrolysed to release monosaccharides.
- Branched structure: Provides multiple terminal ends simultaneously for rapid enzyme action (faster hydrolysis).
- Insoluble: Has no osmotic effect on the cell and cannot easily diffuse out of the cell.
💡 Key Knowledge
Glycogen is the main energy storage molecule in animals. Always link a structural feature explicitly to a functional advantage. For instance, never just state "it is branched"—you must explain that branching creates more ends for faster enzyme hydrolysis to release glucose during high respiration demand.
🧠 Exam Technique
This is a classic "structure-function" question worth up to 4 marks. Aim to make 4 distinct, paired points linking feature and function. Avoid vague statements like "it stores energy well"—specify that it provides a respiratory substrate for energy release.
❌ Common Errors
Students frequently confuse glycogen with cellulose or starch, mistakenly attributing plant-specific properties (like microfibrils or rigidity) to glycogen. Another common error is stating glycogen "is insoluble so it doesn't dissolve" without mentioning the vital consequence regarding water potential/osmosis.
Name the type of peptidase which will hydrolyse the bond labelled G in Figure 5.
✅ Correct Answer
Endopeptidase (accept correct phonetic spelling like endopeptidase).
💡 Key Knowledge
Endopeptidases hydrolyse peptide bonds within the central region of a polypeptide chain, producing smaller peptide fragments. Conversely, exopeptidases hydrolyse peptide bonds at the terminal ends of proteins to remove single amino acids.
Give the number of different R groups in the polypeptide shown in Figure 5.
✅ Correct Answer
3
💡 Key Knowledge
Figure 5 uses distinct geometric shapes (circles, triangles, squares) to represent different amino acids. Counting the unique shapes reveals how many types of monomer are present, which directly corresponds to the number of different R groups.
Use the information in Table 1 to calculate the number of polypeptides: 6 amino acids in length, and 20 amino acids in length.
📐 Step-by-Step Calculation
Total starting length: 101 amino acids.
Step 1: Calculate total amino acids accounted for by known rows in Table 1.
- Length 5 polypeptides: 2 polypeptides × 5 amino acids = 10 amino acids.
- Length 15 polypeptides: 3 polypeptides × 15 amino acids = 45 amino acids.
- Total accounted for = 10 + 45 = 55 amino acids.
Step 2: Find remaining amino acids for lengths 6 and 20.
101 - 55 = 46 remaining amino acids.
Step 3: Solve using the remaining constraints.
We need a combination of length 6 and length 20 polypeptides that sum to 46 amino acids. Testing possible integer values for the number of length-20 polypeptides:
- If 1 × 20-mer = 20 amino acids. Remaining = 26 (not divisible by 6).
- If 2 × 20-mers = 40 amino acids. Remaining = 6 amino acids. This means exactly 1 × 6-mer.
Final Answers:
- 6 amino acids in length = 1
- 20 amino acids in length = 2
❌ Common Calculation Traps & Partial Marks
Students often forget to multiply the number of amino acids per peptide by the frequency of polypeptides given in the table. If you correctly calculated total amino acids accounted for (55) but couldn't solve the final split, the mark scheme awards 1 mark as a consolation for showing working (2 × 5 + 3 × 15) .
Topics
Biology · 3.1 Biological molecules
Question and mark scheme from the AQA AS Level Biology examination, Paper 1, November 2021. QuestionVault is an independent revision resource; questions remain the copyright of the awarding body.