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1.

(a)

A B C D

Phosphate Deoxyribose (Organic) base / thymine / adenine; Hydrogen bond / H bond; 4

(b)

Total percentage of C + G = 84 %; Therefore T will be (100 84) 2; = 8%; 3

(c)

(i)

CGC\AGU\ACG;; [all correct = 2 marks, 1 error1 mark]

(ii)

3;

1
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2.

(a)

1. 2. 3. 4. 5. 6.

(mRNA) is a copy of DNA ; (copy of) part of DNA / eq ; (copy of) one strand / sense strand ; mRNA is complementary (to DNA) / mRNA made up of complementary bases ; mRNA strand, built / formed (looking for idea that mRNA strand is put together during the process) / reference to enzyme ; carries genetic code to, cytoplasm / out of nucleus / to ribosome ; genetic information / base sequence / code, in mRNA determines amino acid sequence ; codons / base triplet on mRNA ; determines amino acid ; (codons) pair with, complementary triplet / anticodons, on tRNA ; reference to start / stop codons / sequences / binding sequences ; occurs on ribosomes ;

(b)

1. 2. 3. 4. 5. 6.

3
[6]

3.

(a) (b)

CCUU; Anticodon;

1 1

(c)

1. 2. 3. 4.

About 20 amino acids; (Triplet) gives 64 permutations / 43; Of 4 bases; (Lowest number of bases with) enough permutations / calculation shown / one or two base mot enough permutations / more codes than needed; Code is degenerate / some amino acids have more than one code; Ensure that the correct amino acid (added to polypeptide) / converse; For given {anticodon / codon (on mRNA)} / eq; Reference to correct sequence of amino acids / correct polypeptide structure; Reference to complimentary base pairing; 1. 2. 3. 4. 5. 6. Radioactivity in protein rises sharply / eq; Then falls (more) slowly; Protein peaks between 5 and 7 minutes; Radioactivity in RNA falls throughout; Compare rate before and after about 5 minutes; Reference to a relationship between protein and RNA; Amino acids (had been) taken up (first) by tRNA; tRNA {delivered / released} amino acids {at ribosome / passed to polypeptide}; Became part of protein (during translation); 2
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5. (d) 1. 2. 3. 4. (e) (i)

(ii)

1. 2. 3.

4.

(a)

1. 2. 3. 4. 5.

Contains (r)RNA; And protein; Has two (sub-)units; Binding{site/groove} to accept RNA; 20-30 nm in size; 2

(b)

Glycine; Lysine;

H
(c) (i)

R N C H

O C

H N

R C H C

O OH

Correct amino acid parts on either side;; Carbon nitrogen back bone; (ii) Condensation

3 1
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5.

(a)

(i) (ii)

Nucleus / nucleoplasm; [allow nucleolus] Condensation / polymerisation 6;

1 1 1

(b)

(i) (ii)

GCT TGG CGG GCT TAG TGG;; [all correct = 2 marks, one error = 1 mark, more than one error = 0 marks] 2

(c)

Reference to start codon; Reference to stop codon; Reference to post transcription modification; 1. 2. 3. 4. 5. 6. 7. 8. Occurs {on / in} ribosome; Two tRNA molecules (held in position in ribosome); Each carrying a specific amino acid; Anticodons on tRNA; Reference to binding of tRNA to complementary bases on mRNA; Peptide bonds form between amino acids; Ribosome moves along mRNA; Until a stop codon is reached

(d)

5
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6.

(a)

PQRS mRNA; tRNA; amino acid; anticodon; DNA Transcription mRNA / messenger RNA Translation Complementary Uracil Guanine Peptide [1 mark for each two correct]

(b)

4
[8]

7.

(a) (b)

Ring drawn around one phosphate, one sugar and one base (linked together); 1. 2. 3. 4. 5. 6. 7. 8. Part of the DNA molecule unwinds; DNA strands {separate / unzips / H-bonds break}; (Mono)nucleotides line up against their complementary bases; Against {sense / one} strand; Reference to RNA polymerase; Individual mononucleotides join up by [condensation reactions / (phosphodi)ester bonds}; mRNA strands separate from DNA molecule; mRNA migrates into cytoplasm / eq; Ribosomes / rough endoplasmic reticulum; Ring drawn around U C G;

5 1 1
[8]

(c)

(i) (ii)

8.

(a)

(i) (ii)

Relates to the sequence of amino acids / eq; 1. 2. 3. Reference to R groups; Reference to (specific) folding of the chain / tertiary structure / eq; Reference to named bonds [not peptide];

(b)

1. 2. 3.

Enzymes have a (specific) active site; Will only fit substrate with the correct shape / eq; Reference to lock & key / enzyme-substrate complexes / induced fit; Correct reference to translation; mRNA lines up at the ribosome / eq; tRNA attaches to specific amino acids / eq; Codon - anticodon binding / complementary base pairing between mRNA and tRNA; Peptide bond; Correct reference to start / stop codons; 4
[9]

(c)

1. 2. 3. 4. 5. 6.

9.

(a)

(i)

COOH group; NH2 group; ACCEPT correct structures drawn out An explanation to include three from: 1. 2. 3. 4. 5. appropriate reference to {secondary structure / -helix or -pleated sheet}; polypeptide chain folded in a specific shape / reference to tertiary structure; reference to R groups; bonding between R groups determines the shape; named bond ie. hydrogen, disulphide, ionic;

(ii)

3 1 1 2
[9]

(b)

(i) (ii) (iii)

6; transcription; AUG CCA UAC GGU UGG AAG;; [1 mark if T instead of U given]

10.

(a)

A phosphate B deoxyribose; (i) Adenine 29, Guanine 21, Cytosine 21;

1 1

(b)

(ii)

1. 2. 3. 4.

a purine always bonds to a pyrimidine; % thymine must equal % adenine / eq; guanine and cytosine must make up rest of molecule / eq; % guanine = % cytosine / eq; max 3

(c)

1. 2. 3. 4. 5.

DNA contains genetic information / eq; DNA codes for protein / eq; a change in DNA could produce a different {protein / mRNA} / eq; idea that it is required throughout life (or {cell / organism}); idea that it is needed to pass on to next generation (of {cell / organism}); part of the DNA (molecule) unwinds; DNA strands separate / {hydrogen / H} bonds break; idea only one strand acts as a template; (free) nucleotides line up against DNA; OR reference to complementary base pairing / correct description; correct reference to RNA polymerase; reference to {nucleotides joining together / formation of phosphodiester bonds}; (to form) mRNA; exits through nuclear pore / from nucleus to cytoplasm / movement to ribosomes; max 5
[12]

max 2

(d)

1. 2. 3. 4. 5. 6. 7. 8.

11.

(a)

1. 2. 3. 4. 5. 6. 7. 8.

idea that part of the DNA helix unwinds; DNA strands separate; hydrogen bonds are broken; idea of one strand acting as a template; (RNA) (mono)nucleotides line up against complementary (DNA) bases; reference to formation of phosphodiester bonds / eq; correct reference to {RNA polymerase / DNA helicase}; reference to detachment of mRNA (molecule) from the DNA; max 4

(b)

1. 2. 3. 4. 5. 6.

reference to translation / eq; mRNA becomes {associated / eq} with ribosomes; idea that a ribosome hold two transfer RNA molecules; reference to transfer RNA attached to amino acid; peptide bonds formed (between adjacent amino acids); reference to ribosome moving along mRNA; GGG CGC UCG AAA;; [1 mistake : 1 mark] 2 max 3

(c)

(i)

(ii)

(glycine) arginine serine lysine;; [1 mistake = 1 mark] 2 1


[12]

(iii)

ATT / ATC / ACT;

12.

(a)

(i)

1. 2. 3.

active {transport / uptake}; facilitated diffusion; endocytosis / pinocytosis / endopinocytosis / eq; max 2 1 1 1

(ii) (b) (i) (ii) (c) 1. 2. 3. 4.

translation; 299; 906; {ATP / ADP / Pi / (inorganic) phosphate}; mRNA; tRNA; rRNA;

max 2
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13.

(a)

(i)

W Guanine / G; X Nucleotide; Y Phosphate / phosphoric acid; Z Deoxyribose / pentose sugar / 5C sugar; max 4 1 1 1

(ii) (b) (i) (ii) (iii)

Hydrogen; Transcription; Aspartic acid, Arginine, Cysteine, Lysine; 1. 2. 3. 4. 5. Incorrect amino acid inserted into polypeptide chain / {chain / sequence} of amino acids changed; Named {Gly / glycine}; Different {side group / R group / eq}; Different bonds formed; Different (3D) shape when folded / eq;

3
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14.

(a) Statement Is a polymer Glycosidic bonds are present Is an energy store in animal cells Has high solubility in water [One mark for every two correct] Starch Glycogen Monosaccharide

(b)

30;

(c)

1. 2. 3. 4. 5. 6. 7. 8. 9.

DNA {uncoils / separates / unzips} / hydrogen bonds break / eq; (Template) strand used to form {mRNA / complementary strand} / transcription; Reference to RNA polymerase; mRNA passes {to ribosome / out of nucleus / to the cytoplasm}; tRNA picks up specific amino acid; Codon and anticodon binding; Correct reference to {start / stop} codons; Peptide bonds forming between amino acids; Example of correct complementary base pairing; 5

(d)

(Different) R groups; Determine bonds formed between R groups of different amino acids; Named bond between R groups, e.g. S=S / H / etc; [not peptide] Reference to {secondary / tertiary} structure; 2
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15.

(a) (b) (c)

Breaks the hydrogen bonds (between the strands) ; Condensation / polymerisation ; Interphase / S phase / synthesis phase ;

1 1 1
[3]

16.

(a)

(i)

Uracil and cytosine (or vice versa); ACCEPT U and C 1 1

(ii) (b)

C T A G C A C;

200 3 / 600; 50; 12 seconds; 3

(c)

1. 2. 3. 4. 5. 6. 7. 8.

The mRNA {attaches /eq} to a ribosome; two tRNA molecules (held in ribosome) / eq; tRNA carries one {specific / eq} amino acid; ref to anticodons on tRNA; (which bind to) {complementary bases / codons} on mRNA; peptide bonds form between amino acids; idea of ribosome moves relative to mRNA; until a stop codon is reached; {DNA / bacterial chromosome} is in the cytoplasm / not in a nucleus; idea of mRNA doesnt have to travel / ribosomes bind straight away; (because) {transcription / mRNA formed) in the cytoplasm; 2
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(d)

1. 2. 3.

17.

(a)

(i)

E: phosphate; F: ribose; G: uracil; nucleus; Tyr, Val, Glu, Arg;; translation;

3 1 2 1
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(ii) (b) (i) (ii)

18.

(a)

(i)

CH 2 OH HO H O H OH H H OH OH H H OH

CH 2 OH O H OH H
glucose

H OH

H OH

galactose;

10

(ii)

1. 2. 3.

breaking of (glycosidic) bond / eq; {addition of / using} water / eq; breaking larger molecule(s) into smaller molecules / named example other than lactose to glucose and galactose OR disaccharide being broken into two monosaccharides; reference to {hydrolytic / named} enzyme; Parents genotypes : Gg / gG for both parents and parents gametes: G g for both parents; Possible genotypes of second child: GG Gg Gg gg; 3 max 2

4. (b) (i) 1.

2. 3.

Probability of not having the condition: 0.75 / 75% / ; more than one {triplet / codon / eq} may code for same amino acid; third base in {triplet / eq} often not important / eq; at 3rd base {point mutation / base changes / eq}; amino acid swapped but does not change shape of protein / eq; (mutation occurs) in intron / eq; risk of miscarriage; risk of harm to {fetus / eq} / eq; reference to a fetus right to life; should the pregnancy be terminated / eq; {practical / financial} issues; mental and emotional issues;

(ii)

1. 2. 3. 4. 5.

max 2

(iii)

1. 2. 3. 4. 5. 6.

max 3
[12]

19.

(a)

Arginine alanine threonine glutamine glycine Accept arg ala thr glu gly 2 [All correct = 2 marks, one mistake = 1 mark, more mistakes = no marks] 2

(b)

ACT Accept adenine cytosine thymine thiamine 1

11

(c)

AGA GCC ACC CAG GGU [All correct = 2 marks, one mistake = 1 mark, more than one mistake = no marks] 2

(d)

(i)

Award one mark for each of the following points in context to a maximum of two marks. 1. 2. 3. alanine would replace threonine; {primary/secondary} structure would be altered; 3D shape would not be correct / eq; Max 2

(ii)

Award one mark for each of the following points in context to a maximum of two marks. 1. 2. 3. a stop signal would be inserted; the protein would be shorter/eq; protein would be 46 amino acids long/eq; Max 2
[9]

20.

(a) (b)

7 Repeat experiment at a range of pH values at closer intervals / at smaller intervals of pH /eq (on either side of the optimum)

1 1

(c)

In very /eq acidic conditions / high concentration of H+; Reference to changes in R group ionisation /eq Bonding disrupted /eq; Enzyme / active site changes shape / tertiary structure changes denaturation ; Substrate / urea does not bond /eq with active site; 3

(d)

Shape affected more at pH 9 than 8 / more denaturation at pH9 than 8 H converse ; Enzyme-substrate complex formed less efficiently / eq 2

12

(e)

Use (buffer solution) pH7 throughout / optimum pH ; Same / stated concentration / volume of urea / substrate Range of concentrations of urease / enzyme; Use the same / stated volume of urease / enzyme; Named variable (e.g. time / temperature / volume of buffer) kept constant Max 4
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21.

(a)

pH ; enzyme concentration ; enzyme (solution) volume ; substrate (solution) volume ; total volume ; more collisions / complexes ; with, enzyme / active site (and substrate) ; in unit time / eq ; enzymes are working as fast as they can / reference to Vmax ; all active sites occupied / eq ; substrate concentration is no longer a limiting factor ; enzyme concentration is limiting ; line on graph begins at zero and is below original line ; less kinetic energy / molecules moving more slowly ; fewer collisions (between enzyme and substrate) ; less energetic collisions ; in unit time / eq ;

(b)

(c)

(d)

3
[9]

22.

Catalysts ; Activation energy ; Substrate ; Active site ; Temperature / non-active site-directed inhibitors ; Change / increase or decrease ; [only accept decrease if referring to inhibitor]
[6]

13

23.

(a)

1. 2. 3. 4. 5.

(Prepare) a range of concentrations of amylase; {Known concentration / excess} {substrate / starch}; Named controlled variables (e.g. temperature); Detail of measuring method; Calculation of rate / reference to timing; Increased rate with increased concentration; More active sites; More collisions with substrate molecules; More enzyme substrate complexes per unit time; Inaccurate measurements / experimental error / small number of readings; Specific reference to difficulty of measuring end point; Explanation of curve e.g. substrate becomes limiting / not a directly proportional relationship; Reference to other variable; 3 3 4

(b)

1. 2. 3. 4.

(c)

1. 2. 3. 4.

(d)

1. 2. 3.

Enzyme specificity / cellulase will not break down starch; Shape of active site; Reference to different bonds in cellulose and starch / and glucose; 2
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24.

(a)

Catalyst:

1. (Chemical that) {speeds up / increases rate of} a reaction; 2. Without itself being changed / used over and over again / not used up;

Activation energy:

3. Energy needed for a chemical reaction to begin; 4. Enzymes reduce it; 4

14

(b)

(i) (ii) (iii)

Hydrolysis; Glycosidic (-1,4) 1. 2. 3. 4. 5. Use water as basis to compare effect; Copper sulphate decreases rate of cellulose breakdown; {Increase in concentration / higher concentrations) decreases rate of breakdown even more; After six days more cellulose broken down at lower concentrations; Credit manipulations of data to compare breakdown of solutions at different concentrations Disulphide bonds maintain {(tertiary/3D)structure/shape}; If disulphide bonds break, the active site will be altered; Cellulose will no longer fit into the active site / eq; Cellulose will not be digested; As copper ions increase more enzymes are affected; Reference to non-active site directed inhibitor;

1 1

(iv)

1. 2. 3. 4. 5. 6.

3
[12]

25.

(a)

(i) (ii) (iii)

Water; Active site; Glycosidic bond; Sucrase {has a (specific) tertiary structure / is a protein}; Reference to specific shape of active site; Only sucrose will fit (the active site of sucrase) / enzymes are specific to substrate / correct reference to lock and key; Form an enzyme-substrate complex; Correct reference to induced fit;

1 1 1

(b)

(i)

15

(ii)

Facilitated diffusion; Use of (specific carrier) proteins / moves molecule down a concentration gradient / correct reference to kinetic theory; OR Active transport; Use of (specific) carrier proteins / moves molecules against a gradient / uses {ATP / energy}; OR Endocytosis; Description of endocytosis e.g. formation of vesicle / use of ATP / eq; 2
[8]

Named bond between R groups, e.g. S=S / H / etc; [not peptide] Reference to {secondary / tertiary} structure; 2
[12]

26.

(a)

(i) (ii)

CN H; peptide

1 1

(b)

An explanation to include two from: 1. 2. 3. 4. chain folds into secondary structure / reference to a-helix or 3 pleated sheets then folds into tertiary structure [ / interactions) between R groups reference to named bond 2

Reject peptide (c) (i) An explanation to include: 1. 2. substrate concentration limiting the rate / eq or converse correct reference to not all active sites occupied by substrate / eq

16

(d)

An outline to include four from: 1. 2. 3. 4. 5. 6. 7. identify independent variable and dependent variable select suitable range of concentrations (at least 5); fixed volumes of enzyme / substrate control of named variable(s) description of apparatus used correct method of obtaining quantitative results reference to replication / calculation of rate / mean values 4
[10]

27.

(a)

1. 2. 3. 4. 5. 6.

Ref to cellulose; Cellulose arranged into microfibrils; Embedded into a matrix; Named component of matrix e.g. pectin / hemicellulose; Ref to {primary and secondary cell walls / several layers of microfibrils}; Ref to plasmodesmata; Cells damaged / some cell content released (during blending) / some of the added water coming through / eq; 1. 2. 3. 4. Enzyme A and enzyme B (both) increase the yield of apple juice; Both enzymes yield similar volumes of apple juice/eq; A combination of enzymes yields a greater volume of juice than either enzyme on its own /eq; Ref to any correctly manipulated figures; 2 3

(b)

(i)

(ii)

17

(iii)

1. 2. 3. 4. 5. 6. 7. 8.

Disrupt the cell wall /eq; {Breakdown / digest} the {pectin I cellulose /eq}; ref to glycosidic bonds being broken; Resulting in an increase in permeability / juice able to leak out of cells /eq; (one) enzyme could be pectinase; (other) enzyme could be cellulase; Enzyme A breaks down a different component (or named component) to enzyme B; Two enzymes together destroy more molecules / cell wall; 4
[10]

28.

(a) (b)

energy / glucose storage; (i) diagram showing 1 glucose molecule / monosaccharide; diagram shows H and OH groups on each of carbon 1 and carbon 4; ref to specificity / shape; correct ref to active site on enzyme; correct ref to enzyme-substrate complex / eq; lock and key concept / induced fit; ref to amino acids in proteins versus glucose in glycogen / peptide versus glycosidic bonds;

(ii)

(c)

reduces activation energy / provides an alternative reaction pathway; (biological) catalyst / speeds up reaction without being used up; allows reactions to occur rapidly at body/lower temperature;

2
[8]

29.

(a)

(i)

1. 2. 3.

(waxy layer) is waterproof; {enzyme / pectinase} in (aqueous) solution; (therefore) {enzyme / pectinase} unable to pass through (waxy layer) / unable to get to {pectin / polysaccharide / carbohydrate} / eq; pectinase is specific and will not digest lipid / waxy surface; shape of (enzyme / pectinase) active site; fits pectin / does not fit cellulose / reference to specificity of enzymes; 2 max 2

4.

(ii)

1. 2.

18

(b)

(i)

1. 2.

increases the surface area; more {substrate /pectin} available / increases the number of {enzyme-substrate complexes / collisions between enzyme / eq and substrate / eq}; hydrolysis uses up water; evaporation of water /eq; idea of same number of the {enzyme / pectinase} molecules but in less {solvent/water}; pectinase released from orange tissues/eq; correct reference to osmosis (into orange); max 2
[8]

(ii)

1. 2. 3. 4. 5.

30.

(a)

(i)

1. 2. 3. 4.

(one of) {alternative / different} forms of a gene / eq; reference to responsible for determining different varieties of one characteristic; idea of each allele has unique sequence of bases; (allele)situated at a (gene) locus / eq; appearance / characteristics (of an organism) / eq; depends on genotype and environment; 2 max 2

(ii)

1. 2.

(b)

1. 2. 3.

gametes shown correctly; genotypes of offspring; probability = 0.33 / / 33%; idea that ears etc., have a lower temperature (than the rest of body); (therefore) enzyme is {active / not denatured / eq}; pigment produced / eq; no pigment produced in other parts because enzyme is {inactive / denatured} / eq; max 3
[10]

(c)

1. 2. 3. 4.

19