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(a)
A B C D
(b)
(c)
(i)
(ii)
3;
1
[10]
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
[12]
(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
[8]
5.
(a)
(i) (ii)
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
[12]
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)
6; transcription; AUG CCA UAC GGU UGG AAG;; [1 mark if T instead of U given]
10.
(a)
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)
(iii)
12.
(a)
(i)
1. 2. 3.
active {transport / uptake}; facilitated diffusion; endocytosis / pinocytosis / endopinocytosis / eq; max 2 1 1 1
translation; 299; 906; {ATP / ADP / Pi / (inorganic) phosphate}; mRNA; tRNA; rRNA;
max 2
[7]
13.
(a)
(i)
W Guanine / G; X Nucleotide; Y Phosphate / phosphoric acid; Z Deoxyribose / pentose sugar / 5C sugar; max 4 1 1 1
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
[10]
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
[12]
15.
Breaks the hydrogen bonds (between the strands) ; Condensation / polymerisation ; Interphase / S phase / synthesis phase ;
1 1 1
[3]
16.
(a)
(i)
(ii) (b)
C T A G C A C;
(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
[12]
(d)
1. 2. 3.
17.
(a)
(i)
3 1 2 1
[7]
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)
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
[11]
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
[12]
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:
14
(b)
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)
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