Genetic Variation Exam Qs Flashcards
Define species richness (1 mark)
Species richness is the number of different species represented in an ecological community, landscape or region
Species richness and an index of diversity can be used to measure biodiversity within a
community.
What is the difference between these two measures of biodiversity? (1 mark)
Species richness measures only number of (different) species / does not measure
number of individuals.
Give two assumptions made when using the mark-release-recapture method. (2 marks)
- No emigration / immigration;
- No losses to predation;
- Marking does not affect survival;
- Birth rate and death rate equal;
- (In this case) all belong to one population.
Suggest the advantage of using the fluorescent powder in the mark release recapture method. (2 marks)
- Only glows brightly with UV, so doesn’t make insects more visible;
- So doesn’t affect / increase predation;
OR - Glows brightly with UV marking visible;
- So makes it easy to pick out labelled insects.
What two measurements are needed to calculate an index of diversity? (2 marks)
Number of (individuals of) each species;
Total number of individuals / number of species
What is speciation? (1 mark)
Speciation is the evolutionary process by which populations evolve to become distinct species.
A mutation of a tumour suppressor gene can result in the formation of a tumour.
Explain how. (2 marks)
- (Tumour suppressor) gene inactivated / not able to control / slow down cell division;
- Rate of cell division too fast / out of control.
Not all mutations result in a change to the amino acid sequence of the encoded polypeptide.
Explain why. (2 marks)
- (Genetic) code degenerate;
2. Mutation in intron.
Use your knowledge of monoclonal antibodies to suggest how this antibody stops
the growth of a tumour. (3 marks)
- Antibody has specific tertiary structure / binding site / variable region;
- Complementary (shape / fit) to receptor protein / GF / binds to receptor protein / to GF;
- Prevents GF binding (to receptor).
Messenger RNA (mRNA) is used during translation to form polypeptides. Describe how mRNA is produced in the nucleus of a cell. (6 marks)
- Helicase;
- Breaks hydrogen bonds;
- Only one DNA strand acts as template;
- RNA nucleotides attracted to exposed bases;
- (Attraction) according to base pairing rule;
- RNA polymerase joins (RNA) nucleotides together;
- Pre-mRNA spliced to remove introns.
Describe the structure of proteins. (6 marks)
- Polymer of amino acids;
- Joined by peptide bonds;
- Formed by condensation;
- Primary structure is order of amino acids;
- Secondary structure is folding of polypeptide chain due to hydrogen bonding;
- Tertiary structure is 3-D folding due to hydrogen bonding and ionic /
disulfide bonds; - Quaternary structure is two or more polypeptide chains
Describe how proteins are digested in the human gut. (4 marks)
- Hydrolysis of peptide bonds;
- Endopeptidases break polypeptides into smaller peptide chains;
- Exopeptidases remove terminal amino acids;
- Dipeptidases hydrolyse / break down dipeptides into amino acids.
One form of mitochondrial disease is caused by a mutation of a mitochondrial gene that codes for a tRNA. The mutation involves substitution of guanine for
adenine in the DNA base sequence. This changes the anticodon on the tRNA. This results in the formation of a non-functional protein in the mitochondrion.
Suggest how the change in an anticodon of a tRNA leads to MD (3 marks)
- Change to tRNA leads to wrong amino acid being incorporated into
protein; - Tertiary structure (of protein) changed;
- Protein required for oxidative phosphorylation / the Krebs cycle, so less /
no ATP made.
Messenger RNA (mRNA) is used during translation to form polypeptides. Describe how mRNA is produced in the nucleus of a cell. (6 marks)
- Helicase;
- Breaks hydrogen bonds;
- Only one DNA strand acts as template;
- RNA nucleotides attracted to exposed bases;
- (Attraction) according to base pairing rule;
- RNA polymerase joins (RNA) nucleotides together;
- Pre-mRNA spliced to remove introns
Describe the structure of proteins. (5 marks)
- Polymer of amino acids;
- Joined by peptide bonds;
- Formed by condensation;
- Primary structure is order of amino acids;
- Secondary structure is folding of polypeptide chain due to hydrogen bonding
- Tertiary structure is 3-D folding due to hydrogen bonding and ionic /
disulfide bonds; - Quaternary structure is two or more polypeptide chains.
Describe how proteins are digested in the human gut. (4 marks)
- Hydrolysis of peptide bonds;
- Endopeptidases break polypeptides into smaller peptide chains;
- Exopeptidases remove terminal amino acids;
- Dipeptidases hydrolyse/break down dipeptides into amino acids.
Mitochondrial disease (MD) often causes muscle weakness. Use your knowledge of respiration and muscle contraction to suggest explanations for this
effect of MD
(3 marks)
- Reduction in ATP production by aerobic respiration;
- Less force generated because fewer actin and myosin interactions in
muscle; - Fatigue caused by lactate from anaerobic respiration.