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A Level H2 Biology Practice Paper 1
Free A Level H2 Biology Practice Paper 1, Exam version, with questions, answers, and A Level-style practice for Singapore students.
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TuitionGoWhere Practice Paper - Biology H2 A-Level - Mark Scheme
Total Marks: 75
Section A [25 marks]
Question 1
(a) (i) Identify the structures labelled A, B, C and D. [4]
- A: Nucleus [1]
- B: Mitochondrion [1]
- C: Rough endoplasmic reticulum / RER [1]
- D: Ribosomes [1]
(ii) State the magnification used if the actual diameter of structure A is 8 μm and its diameter in the micrograph is 32 mm. [2]
- Convert units: 32 mm = 32,000 μm [1]
- Magnification = 32,000 ÷ 8 = ×4000 [1]
(b) With reference to Fig. 1.1, explain how structure B is adapted for its role in aerobic respiration. [4]
- Inner membrane folded into cristae [1]
- Increases surface area for electron transport chain / ATP synthesis [1]
- Matrix contains enzymes for Krebs cycle [1]
- Double membrane allows compartmentalization / proton gradient formation [1]
Question 2
(a) Describe and explain how gel electrophoresis is used to diagnose sickle cell anaemia. [4]
- Electric field / potential difference applied across gel [1]
- Proteins move according to charge and molecular mass [1]
- Normal haemoglobin (HbA) and sickle haemoglobin (HbS) migrate differently [1]
- Different migration patterns allow identification of genotype [1]
(b) With reference to Fig. 2.1, explain the different numbers of fragments seen in different individuals. [3]
- Different alleles produce proteins of different sizes/charges [1]
- Heterozygotes carry two different alleles, so show two bands [1]
- Homozygotes carry identical alleles, so show one band [1]
(c) Identify which individual(s) would be expected to show symptoms of sickle cell anaemia. Explain your answer. [2]
- Individual(s): Individual 3 [1]
- Explanation: Shows only one band in position of HbS / is homozygous for sickle cell allele [1]
Question 3
(a) Describe how you would test for the presence of starch. [2]
- Add iodine solution [1]
- Blue-black colour indicates presence of starch [1]
(b) (i) Explain the shape of the curve between points X and Y. [3]
- Increasing substrate concentration increases rate of reaction [1]
- More substrate molecules available for enzyme active sites [1]
- More enzyme-substrate complexes formed per unit time [1]
(ii) Explain why the curve levels off after point Y. [2]
- All enzyme active sites are occupied / enzyme is saturated [1]
- Further increase in substrate concentration has no effect on rate [1]
Section B [25 marks]
Question 4
(a) The lac operon codes for inducible enzymes. Explain why it is advantageous for E. coli to have an inducible operon for lactose metabolism. [3]
- Enzymes only produced when lactose is present [1]
- Saves energy/resources when lactose is absent [1]
- Allows rapid response to lactose availability [1]
(b) (i) lactose is absent from the growth medium [4]
- Repressor protein binds to operator [1]
- RNA polymerase cannot bind to promoter / transcription blocked [1]
- No mRNA produced [1]
- No enzymes for lactose metabolism produced [1]
(ii) lactose is present in the growth medium [4]
- Lactose acts as inducer / binds to repressor protein [1]
- Repressor protein changes shape / cannot bind to operator [1]
- RNA polymerase can bind to promoter [1]
- Transcription occurs / enzymes for lactose metabolism produced [1]
Question 5
(a) Explain why oxygen concentration decreases after the addition of glucose at point A. [3]
- Glucose provides substrate for respiration [1]
- Oxygen is used as final electron acceptor in electron transport chain [1]
- Rate of oxygen consumption increases [1]
(b) Sodium azide is an inhibitor of cytochrome oxidase in the electron transport chain. With reference to Fig. 5.1, explain the effect of adding sodium azide at point B. [4]
- Electron transport chain is blocked [1]
- Oxygen cannot accept electrons / is not reduced [1]
- Oxygen consumption stops [1]
- Oxygen concentration increases as it is no longer being used [1]
(c) Calculate the rate of oxygen consumption between 2 and 4 minutes. [2]
- Change in oxygen concentration = (reading at 4 min) - (reading at 2 min) [1]
- Rate = change ÷ time = change ÷ 2 minutes [1] Note: Specific values depend on graph scale provided
Question 6
Describe the structure of proteins, explaining how the different levels of structure contribute to protein function. [10]
Mark scheme:
- Primary structure: sequence of amino acids joined by peptide bonds [1]
- Determines all higher levels of structure [1]
- Secondary structure: α-helices and β-pleated sheets [1]
- Held by hydrogen bonds between backbone atoms [1]
- Provides structural stability [1]
- Tertiary structure: 3D folding of polypeptide chain [1]
- Held by various bonds (hydrogen, ionic, disulfide, hydrophobic interactions) [1]
- Determines active site shape in enzymes / binding sites [1]
- Quaternary structure: association of multiple polypeptide chains [1]
- Examples: haemoglobin (4 subunits), enzymes with multiple subunits [1]
Section C [25 marks]
Question 7
(a) (i) Using appropriate symbols, write the genotypes of the parent generation. [2]
- Male: C^B C^B [1]
- Female: C^W C^W [1]
(ii) Explain the phenotype of the F1 generation. [2]
- All F1 are C^B C^W (heterozygous) [1]
- Codominance results in blue feathers (intermediate phenotype) [1]
(b) (i) State the null hypothesis for this test. [1]
- The observed results fit the expected 1:2:1 ratio [1]
(ii) Calculate the expected numbers for each phenotype class in the F2 generation. [3]
- Total F2 offspring = 89 + 183 + 94 = 366 [1]
- Expected black: 366 ÷ 4 = 91.5 [1]
- Expected blue: 366 ÷ 2 = 183 [1]
- Expected splashed white: 366 ÷ 4 = 91.5 [1]
(iii) State the conclusion of this test and explain what this means. [2]
- Conclusion: Accept null hypothesis / no significant difference [1]
- Explanation: Observed results fit expected 1:2:1 ratio / genes assort independently [1]
Question 8
(a) With reference to Fig. 8.1, explain the role of electrons as they move from photosystem II to photosystem I. [4]
- Electrons are excited by light energy at PSII [1]
- Move through electron transport chain [1]
- Energy released is used to pump H+ into thylakoid lumen [1]
- Creates proton gradient for ATP synthesis [1]
(b) Explain how the light-dependent reactions of photosynthesis produce ATP. [6]
- Light energy excites electrons in photosystems [1]
- Electrons move through electron transport chain [1]
- Energy released pumps H+ from stroma into thylakoid lumen [1]
- Creates proton gradient across thylakoid membrane [1]
- H+ flow back through ATP synthase [1]
- ADP + Pi → ATP (chemiosmosis) [1]
(c) Describe and explain the effects of an increase in oxygen concentration on the rate of photosynthesis in C3 plants. [5]
- Rate of photosynthesis decreases [1]
- RuBisCO catalyses both carboxylation (with CO2) and oxygenation (with O2) [1]
- High oxygen concentration favours oxygenation of RuBP [1]
- This leads to photorespiration [1]
- Photorespiration produces no ATP or NADPH, reducing net photosynthesis [1]