2.3· 261 questions · 261 marks · 313 min · 2004–2025· Multiple choice
Every Cambridge A Level Biology Paper 1 question on proteins, laid out as 83 A4 pages with the mark scheme below. Nothing is left out. Free to read, no account.





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83 / 83Answers below. Sit the paper first if you are practising.
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
Pastlit
Biology 9700 · Proteins — Paper 1
A Level · topical answer key — answer key (teacher use)
Question
Answer
Marks
| Question | Answer | Marks | From |
|---|---|---|---|
| 1 | B | 1 | 9700/11 Oct/Nov 2004 |
| 2 | A | 1 | 9700/11 Oct/Nov 2004 |
| 3 | C | 1 | 9700/11 May/June 2006 |
| 4 | C | 1 | 9700/11 May/June 2006 |
| 5 | B | 1 | 9700/11 Oct/Nov 2006 |
| 6 | C | 1 | 9700/11 Oct/Nov 2006 |
| 7 | D | 1 | 9700/11 Oct/Nov 2006 |
| 8 | A | 1 | 9700/11 Oct/Nov 2006 |
| 9 | D | 1 | 9700/11 Oct/Nov 2007 |
| 10 | B | 1 | 9700/11 Oct/Nov 2007 |
| 11 | D | 1 | 9700/11 Oct/Nov 2007 |
| 12 | B | 1 | 9700/11 May/June 2008 |
| 13 | D | 1 | 9700/11 May/June 2008 |
| 14 | B | 1 | 9700/11 May/June 2008 |
| 15 | C | 1 | 9700/11 Oct/Nov 2008 |
| 16 | A | 1 | 9700/11 Oct/Nov 2008 |
| 17 | B | 1 | 9700/11 Oct/Nov 2008 |
| 18 | A | 1 | 9700/11 Oct/Nov 2008 |
| 19 | D | 1 | 9700/12 Oct/Nov 2009 |
| 20 | B | 1 | 9700/12 Oct/Nov 2009 |
| 21 | D | 1 | 9700/12 Oct/Nov 2009 |
| 22 | A | 1 | 9700/12 Oct/Nov 2009 |
| 23 | B | 1 | 9700/12 Oct/Nov 2009 |
| 24 | B | 1 | 9700/11 May/June 2010 |
| 25 | D | 1 | 9700/11 May/June 2010 |
| 26 | B | 1 | 9700/12 May/June 2010 |
| 27 | D | 1 | 9700/12 May/June 2010 |
| 28 | D | 1 | 9700/13 May/June 2010 |
| 29 | B | 1 | 9700/13 May/June 2010 |
| 30 | C | 1 | 9700/12 Oct/Nov 2010 |
| 31 | C | 1 | 9700/12 Oct/Nov 2010 |
| 32 | D | 1 | 9700/12 Oct/Nov 2010 |
| 33 | A | 1 | 9700/11 May/June 2011 |
| 34 | B | 1 | 9700/11 May/June 2011 |
| 35 | A | 1 | 9700/11 May/June 2011 |
| 36 | A | 1 | 9700/11 May/June 2011 |
| 37 | C | 1 | 9700/12 May/June 2011 |
| 38 | D | 1 | 9700/12 May/June 2011 |
| 39 | D | 1 | 9700/12 May/June 2011 |
| 40 | B | 1 | 9700/13 May/June 2011 |
| 41 | A | 1 | 9700/13 May/June 2011 |
| 42 | A | 1 | 9700/13 May/June 2011 |
| 43 | A | 1 | 9700/11 Oct/Nov 2011 |
| 44 | A | 1 | 9700/13 Oct/Nov 2011 |
| 45 | C | 1 | 9700/11 May/June 2012 |
| 46 | B | 1 | 9700/11 May/June 2012 |
| 47 | D | 1 | 9700/12 May/June 2012 |
| 48 | B | 1 | 9700/13 May/June 2012 |
| 49 | C | 1 | 9700/13 May/June 2012 |
| 50 | D | 1 | 9700/11 Oct/Nov 2012 |
| 51 | A | 1 | 9700/11 Oct/Nov 2012 |
| 52 | B | 1 | 9700/12 Oct/Nov 2012 |
| 53 | C | 1 | 9700/12 Oct/Nov 2012 |
| 54 | C | 1 | 9700/12 Oct/Nov 2012 |
| 55 | D | 1 | 9700/13 Oct/Nov 2012 |
| 56 | C | 1 | 9700/11 May/June 2013 |
| 57 | A | 1 | 9700/12 May/June 2013 |
| 58 | C | 1 | 9700/12 May/June 2013 |
| 59 | B | 1 | 9700/12 May/June 2013 |
| 60 | C | 1 | 9700/13 May/June 2013 |
| 61 | B | 1 | 9700/13 May/June 2013 |
| 62 | C | 1 | 9700/11 Oct/Nov 2013 |
| 63 | B | 1 | 9700/11 Oct/Nov 2013 |
| 64 | D | 1 | 9700/11 Oct/Nov 2013 |
| 65 | B | 1 | 9700/11 Oct/Nov 2013 |
| 66 | C | 1 | 9700/12 Oct/Nov 2013 |
| 67 | A | 1 | 9700/12 Oct/Nov 2013 |
| 68 | B | 1 | 9700/12 Oct/Nov 2013 |
| 69 | A | 1 | 9700/13 Oct/Nov 2013 |
| 70 | D | 1 | 9700/13 Oct/Nov 2013 |
| 71 | C | 1 | 9700/11 May/June 2014 |
| 72 | A | 1 | 9700/11 May/June 2014 |
| 73 | C | 1 | 9700/12 May/June 2014 |
| 74 | A | 1 | 9700/12 May/June 2014 |
| 75 | C | 1 | 9700/12 May/June 2014 |
| 76 | C | 1 | 9700/13 May/June 2014 |
| 77 | D | 1 | 9700/13 May/June 2014 |
| 78 | D | 1 | 9700/13 May/June 2014 |
| 79 | C | 1 | 9700/13 May/June 2014 |
| 80 | A | 1 | 9700/11 Oct/Nov 2014 |
| 81 | D | 1 | 9700/11 Oct/Nov 2014 |
| 82 | A | 1 | 9700/12 Oct/Nov 2014 |
| 83 | B | 1 | 9700/12 Oct/Nov 2014 |
| 84 | A | 1 | 9700/12 Oct/Nov 2014 |
| 85 | A | 1 | 9700/12 Oct/Nov 2014 |
| 86 | D | 1 | 9700/13 Oct/Nov 2014 |
| 87 | B | 1 | 9700/13 Oct/Nov 2014 |
| 88 | D | 1 | 9700/11 May/June 2015 |
| 89 | A | 1 | 9700/11 May/June 2015 |
| 90 | B | 1 | 9700/12 May/June 2015 |
| 91 | D | 1 | 9700/12 May/June 2015 |
| 92 | D | 1 | 9700/12 May/June 2015 |
| 93 | C | 1 | 9700/13 May/June 2015 |
| 94 | D | 1 | 9700/13 May/June 2015 |
| 95 | D | 1 | 9700/13 May/June 2015 |
| 96 | C | 1 | 9700/12 Oct/Nov 2015 |
| 97 | B | 1 | 9700/13 Oct/Nov 2015 |
| 98 | A | 1 | 9700/13 Oct/Nov 2015 |
| 99 | B | 1 | 9700/13 Oct/Nov 2015 |
| 100 | D | 1 | 9700/12 Feb/March 2016 |
| 101 | A | 1 | 9700/11 May/June 2016 |
| 102 | C | 1 | 9700/11 May/June 2016 |
| 103 | C | 1 | 9700/12 May/June 2016 |
| 104 | C | 1 | 9700/12 May/June 2016 |
| 105 | A | 1 | 9700/12 May/June 2016 |
| 106 | A | 1 | 9700/12 May/June 2016 |
| 107 | see sheet | 1 | 9700/13 May/June 2016 |
| 108 | C | 1 | 9700/11 Oct/Nov 2016 |
| 109 | D | 1 | 9700/13 Oct/Nov 2016 |
| 110 | A | 1 | 9700/13 Oct/Nov 2016 |
| 111 | C | 1 | 9700/13 Oct/Nov 2016 |
| 112 | D | 1 | 9700/12 Feb/March 2017 |
| 113 | C | 1 | 9700/12 Feb/March 2017 |
| 114 | D | 1 | 9700/12 Feb/March 2017 |
| 115 | B | 1 | 9700/12 Feb/March 2017 |
| 116 | C | 1 | 9700/11 May/June 2017 |
| 117 | B | 1 | 9700/11 May/June 2017 |
| 118 | C | 1 | 9700/12 May/June 2017 |
| 119 | D | 1 | 9700/12 May/June 2017 |
| 120 | D | 1 | 9700/13 May/June 2017 |
| 121 | A | 1 | 9700/13 May/June 2017 |
| 122 | C | 1 | 9700/12 Oct/Nov 2017 |
| 123 | A | 1 | 9700/12 Oct/Nov 2017 |
| 124 | B | 1 | 9700/12 Oct/Nov 2017 |
| 125 | D | 1 | 9700/13 Oct/Nov 2017 |
| 126 | A | 1 | 9700/13 Oct/Nov 2017 |
| 127 | B | 1 | 9700/13 Oct/Nov 2017 |
| 128 | A | 1 | 9700/12 Feb/March 2018 |
| 129 | A | 1 | 9700/12 Feb/March 2018 |
| 130 | B | 1 | 9700/12 Feb/March 2018 |
| 131 | A | 1 | 9700/11 May/June 2018 |
| 132 | A | 1 | 9700/11 May/June 2018 |
| 133 | D | 1 | 9700/11 May/June 2018 |
| 134 | A | 1 | 9700/11 May/June 2018 |
| 135 | C | 1 | 9700/12 May/June 2018 |
| 136 | B | 1 | 9700/12 May/June 2018 |
| 137 | C | 1 | 9700/12 May/June 2018 |
| 138 | D | 1 | 9700/13 May/June 2018 |
| 139 | A | 1 | 9700/13 May/June 2018 |
| 140 | D | 1 | 9700/11 Oct/Nov 2018 |
| 141 | D | 1 | 9700/11 Oct/Nov 2018 |
| 142 | A | 1 | 9700/11 Oct/Nov 2018 |
| 143 | A | 1 | 9700/12 Oct/Nov 2018 |
| 144 | D | 1 | 9700/12 Oct/Nov 2018 |
| 145 | D | 1 | 9700/12 Oct/Nov 2018 |
| 146 | B | 1 | 9700/13 Oct/Nov 2018 |
| 147 | A | 1 | 9700/13 Oct/Nov 2018 |
| 148 | B | 1 | 9700/12 Feb/March 2019 |
| 149 | A | 1 | 9700/12 Feb/March 2019 |
| 150 | B | 1 | 9700/11 May/June 2019 |
| 151 | A | 1 | 9700/12 May/June 2019 |
| 152 | B | 1 | 9700/12 May/June 2019 |
| 153 | B | 1 | 9700/12 May/June 2019 |
| 154 | A | 1 | 9700/13 May/June 2019 |
| 155 | D | 1 | 9700/13 May/June 2019 |
| 156 | C | 1 | 9700/11 Oct/Nov 2019 |
| 157 | B | 1 | 9700/12 Oct/Nov 2019 |
| 158 | B | 1 | 9700/12 Oct/Nov 2019 |
| 159 | D | 1 | 9700/12 Oct/Nov 2019 |
| 160 | C | 1 | 9700/13 Oct/Nov 2019 |
| 161 | B | 1 | 9700/13 Oct/Nov 2019 |
| 162 | C | 1 | 9700/12 Feb/March 2020 |
| 163 | A | 1 | 9700/11 May/June 2020 |
| 164 | A | 1 | 9700/11 May/June 2020 |
| 165 | A | 1 | 9700/11 May/June 2020 |
| 166 | B | 1 | 9700/12 May/June 2020 |
| 167 | D | 1 | 9700/13 May/June 2020 |
| 168 | A | 1 | 9700/13 May/June 2020 |
| 169 | B | 1 | 9700/13 May/June 2020 |
| 170 | D | 1 | 9700/13 May/June 2020 |
| 171 | D | 1 | 9700/11 Oct/Nov 2020 |
| 172 | A | 1 | 9700/11 Oct/Nov 2020 |
| 173 | D | 1 | 9700/11 Oct/Nov 2020 |
| 174 | C | 1 | 9700/13 Oct/Nov 2020 |
| 175 | D | 1 | 9700/13 Oct/Nov 2020 |
| 176 | C | 1 | 9700/13 Oct/Nov 2020 |
| 177 | C | 1 | 9700/12 Feb/March 2021 |
| 178 | B | 1 | 9700/11 May/June 2021 |
| 179 | D | 1 | 9700/11 May/June 2021 |
| 180 | C | 1 | 9700/11 May/June 2021 |
| 181 | D | 1 | 9700/11 May/June 2021 |
| 182 | B | 1 | 9700/12 May/June 2021 |
| 183 | C | 1 | 9700/13 May/June 2021 |
| 184 | B | 1 | 9700/13 May/June 2021 |
| 185 | D | 1 | 9700/13 May/June 2021 |
| 186 | C | 1 | 9700/11 Oct/Nov 2021 |
| 187 | C | 1 | 9700/11 Oct/Nov 2021 |
| 188 | C | 1 | 9700/12 Oct/Nov 2021 |
| 189 | C | 1 | 9700/12 Oct/Nov 2021 |
| 190 | A | 1 | 9700/12 Oct/Nov 2021 |
| 191 | see sheet | 1 | 9700/13 Oct/Nov 2021 |
| 192 | C | 1 | 9700/13 Oct/Nov 2021 |
| 193 | D | 1 | 9700/13 Oct/Nov 2021 |
| 194 | B | 1 | 9700/13 Oct/Nov 2021 |
| 195 | D | 1 | 9700/13 Oct/Nov 2021 |
| 196 | D | 1 | 9700/12 Feb/March 2022 |
| 197 | C | 1 | 9700/12 Feb/March 2022 |
| 198 | C | 1 | 9700/12 Feb/March 2022 |
| 199 | A | 1 | 9700/11 May/June 2022 |
| 200 | C | 1 | 9700/11 May/June 2022 |
| 201 | B | 1 | 9700/11 May/June 2022 |
| 202 | A | 1 | 9700/12 May/June 2022 |
| 203 | B | 1 | 9700/12 May/June 2022 |
| 204 | A | 1 | 9700/12 May/June 2022 |
| 205 | B | 1 | 9700/13 May/June 2022 |
| 206 | B | 1 | 9700/13 May/June 2022 |
| 207 | A | 1 | 9700/13 May/June 2022 |
| 208 | D | 1 | 9700/11 Oct/Nov 2022 |
| 209 | D | 1 | 9700/11 Oct/Nov 2022 |
| 210 | B | 1 | 9700/11 Oct/Nov 2022 |
| 211 | B | 1 | 9700/12 Oct/Nov 2022 |
| 212 | C | 1 | 9700/12 Oct/Nov 2022 |
| 213 | B | 1 | 9700/12 Oct/Nov 2022 |
| 214 | D | 1 | 9700/13 Oct/Nov 2022 |
| 215 | C | 1 | 9700/12 Feb/March 2023 |
| 216 | D | 1 | 9700/12 Feb/March 2023 |
| 217 | C | 1 | 9700/11 May/June 2023 |
| 218 | C | 1 | 9700/11 May/June 2023 |
| 219 | B | 1 | 9700/12 May/June 2023 |
| 220 | B | 1 | 9700/12 May/June 2023 |
| 221 | B | 1 | 9700/13 May/June 2023 |
| 222 | D | 1 | 9700/13 May/June 2023 |
| 223 | D | 1 | 9700/13 May/June 2023 |
| 224 | B | 1 | 9700/13 May/June 2023 |
| 225 | A | 1 | 9700/13 May/June 2023 |
| 226 | A | 1 | 9700/12 Oct/Nov 2023 |
| 227 | D | 1 | 9700/12 Oct/Nov 2023 |
| 228 | B | 1 | 9700/12 Feb/March 2024 |
| 229 | D | 1 | 9700/12 Feb/March 2024 |
| 230 | C | 1 | 9700/11 May/June 2024 |
| 231 | B | 1 | 9700/11 May/June 2024 |
| 232 | D | 1 | 9700/11 May/June 2024 |
| 233 | C | 1 | 9700/11 May/June 2024 |
| 234 | D | 1 | 9700/12 May/June 2024 |
| 235 | B | 1 | 9700/12 May/June 2024 |
| 236 | A | 1 | 9700/12 May/June 2024 |
| 237 | A | 1 | 9700/13 May/June 2024 |
| 238 | C | 1 | 9700/13 May/June 2024 |
| 239 | B | 1 | 9700/11 Oct/Nov 2024 |
| 240 | A | 1 | 9700/12 Oct/Nov 2024 |
| 241 | A | 1 | 9700/12 Oct/Nov 2024 |
| 242 | A | 1 | 9700/12 Oct/Nov 2024 |
| 243 | D | 1 | 9700/13 Oct/Nov 2024 |
| 244 | A | 1 | 9700/13 Oct/Nov 2024 |
| 245 | C | 1 | 9700/13 Oct/Nov 2024 |
| 246 | C | 1 | 9700/12 Feb/March 2025 |
| 247 | B | 1 | 9700/12 Feb/March 2025 |
| 248 | A | 1 | 9700/12 Feb/March 2025 |
| 249 | D | 1 | 9700/12 May/June 2025 |
| 250 | C | 1 | 9700/12 May/June 2025 |
| 251 | B | 1 | 9700/13 May/June 2025 |
| 252 | A | 1 | 9700/13 May/June 2025 |
| 253 | B | 1 | 9700/13 May/June 2025 |
| 254 | D | 1 | 9700/13 May/June 2025 |
| 255 | D | 1 | 9700/14 May/June 2025 |
| 256 | C | 1 | 9700/14 May/June 2025 |
| 257 | D | 1 | 9700/11 Oct/Nov 2025 |
| 258 | B | 1 | 9700/11 Oct/Nov 2025 |
| 259 | A | 1 | 9700/11 Oct/Nov 2025 |
| 260 | A | 1 | 9700/13 Oct/Nov 2025 |
| 261 | C | 1 | 9700/13 Oct/Nov 2025 |
12 Which term describes the type of bonding responsible for stabilising the secondary structure of a protein? A disulphide B hydrogen C hydrophobic D ionic
1 marks
Answer: B
13 How many different polypeptides, each consisting of r amino acids, can be made if the number of different amino acids available is n ? n r r n n A B C n x r D r
1 marks
Answer: A
10 At which levels of protein structure do hydrophobic interactions occur? A primary, secondary and tertiary B primary, secondary, tertiary and quaternary C tertiary and quaternary D quaternary only
1 marks
Answer: C
11 The diagram shows a dipeptide. Which bond is the peptide bond? A B C D R1 O R2 H O N C C N C C H H H H OH
1 marks
Answer: C
6 Which statement is true for cellulose, but not true for protein? A It is found in cell surface membranes. B It is synthesised from identical sub-units. C It is used as an energy source. D It may be a structural component.
1 marks
Answer: B
8 Which level of protein structure maintains the globular shapes of enzymes? A primary B secondary C tertiary D quaternary
1 marks
Answer: C
9 Which type of bond is involved in maintaining primary, secondary and tertiary structure in protein molecules? level of structure primary secondary tertiary A disulphide ionic hydrogen B covalent peptide ionic C ionic disulphide covalent D peptide hydrogen disulphide
1 marks
Answer: D
10 What is the function of iron in the haemoglobin molecule? A It binds oxygen to the haemoglobin molecule. B It makes the haemoglobin more soluble in the red blood cell. C It stabilises the quaternary structure of the protein. D It undergoes reversible oxidation and reduction.
1 marks
Answer: A
7 When solutions of dilute sodium hydroxide and copper(II) sulphate (biuret test) were added to an unknown substance, a purple colour was observed. This test indicates the presence of which bond in the unknown substance? A disulphide B hydrogen C ionic D peptide
1 marks
Answer: D
8 The diagram shows part of a macromolecule in the form of triple helices, lying side by side with covalent cross links between them. What is the name of the molecule? A cellulose B collagen C glycogen D triglyceride
1 marks
Answer: B
12 The diagrams show four different molecules. P Q CH2OH CH2OH C O H O H H N C C H C C H OH OH H H HO OH C C H OH R S CH2OH O OH C O C H OH H CH2 C C OH H H HO H O C C N C C H OH H OH H Which shows the correct information about the molecule or molecules? contains a forms 1,6 glycosidic forms peptide bonds carboxyl group bonds in glycogen by condensation A P P P and Q B Q R P and R C R R R and Q D S P Q and S
1 marks
Answer: D
7 How is the shape of a polypeptide chain maintained when it is coiled into an α helix? A disulphide bonds B hydrogen bonds C hydrophobic interactions D ionic bonds
1 marks
Answer: B
10 What will break an ionic bond between amino acids? A condensation B hydrolysis C low temperature D pH change
1 marks
Answer: D
11 When hydrolysed, which molecules have products containing a carboxyl group? 1 phospholipids 2 polysaccharides 3 proteins A 1 and 2 B 1 and 3 C 2 and 3 D 3 only
1 marks
Answer: B
7 Which substances contain carbon, hydrogen, oxygen and nitrogen? 1 amylopectin 2 collagen 3 deoxyribonucleic acid A 2 only B 1 and 2 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: C
9 A number of different types of bonds maintain the structure of proteins. These include disulphide, hydrogen and ionic bonds, as well as hydrophobic interactions. Some of these are stronger than others. Which are the strongest? A disulphide bonds B hydrogen bonds C hydrophobic interactions D ionic bonds
1 marks
Answer: A
10 Haemoglobin is a globular protein consisting of four polypeptide chains – 2 alpha chains and 2 beta chains. In normal individuals, in the DNA which codes for each beta chain, the sixth triplet has a code for glutamic acid. In individuals with sickle cell anaemia this base triplet changes and codes for valine. What aspect of the haemoglobin molecule does this mutation change? A the iron content B the primary structure C the quaternary structure D the secondary structure
1 marks
Answer: B
11 Which type of molecule contains disulphide bonds and which contains glycosidic bonds? disulphide bonds glycosidic bonds A glycoprotein polysaccharide B nucleic acid glycoprotein C polysaccharide nucleic acid D protein triglyceride
1 marks
Answer: A
7 Which combination of bond types correctly shows the weak and strong bonds that hold a molecule of protein in shape? types of bond hydrogen disulfide ionic A strong strong weak B strong weak strong C weak strong strong D weak strong weak
1 marks
Answer: D
8 Which statement is true for cellulose, but not true for protein? A It is found in cell surface membranes. B It is synthesised from identical sub-units. C It is used as an energy source. D It may be a structural component.
1 marks
Answer: B
10 The diagram shows a tripeptide molecule. H H O H C C C OH H H NH 1 H O H H C C C C 2 O H H 3 NH H H H C C C 4 O H NH2 At which two points will hydrolysis occur to release three amino acids? A 1 and 2 B 1 and 3 C 2 and 3 D 2 and 4
1 marks
Answer: D
12 HIV-1 protease is an enzyme produced by the HIV virus. Two identical chains of 99 amino acids form the enzyme. In each chain, amino acids 25, 26 and 27 in the sequence form part of the active site. Which orders of protein structure control the shape of the active site? A primary, secondary, tertiary and quaternary B primary, secondary and tertiary only C primary and quaternary only D quaternary only
1 marks
Answer: A
13 Which features of collagen result in it having high tensile strength? 1 covalent bonds form between adjacent molecules 2 each three-stranded molecule is held together by hydrogen bonds 3 every third amino acid in the polypeptide is small 4 the primary structure is held together by peptide bonds A 1 and 2 B 1, 2 and 3 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: B
13 Which feature of haemoglobin makes it a globular protein? A It has four cross-linked polypeptide chains forming a quaternary structure. B It has hydrophobic groups on the inside and hydrophilic groups on the outside. C It has hydrophobic interactions and is insoluble in water. D It has polypeptide chains which are cross-linked to form sheets.
1 marks
Answer: B
15 The enzyme lysozyme secreted from tear glands forms deposits on contact lenses. Which ingredient would be effective in a contact lens cleaner for removing these deposits? A ethanol B lysosomes C pH buffers D proteases
1 marks
Answer: D
3 Which feature of haemoglobin makes it a globular protein? A It has four cross-linked polypeptide chains forming a quaternary structure. B It has hydrophobic groups on the inside and hydrophilic groups on the outside. C It has hydrophobic interactions and is insoluble in water. D It has polypeptide chains which are cross-linked to form sheets.
1 marks
Answer: B
25 The enzyme lysozyme secreted from tear glands forms deposits on contact lenses. Which ingredient would be effective in a contact lens cleaner for removing these deposits? A ethanol B lysosomes C pH buffers D proteases
1 marks
Answer: D
1 The enzyme lysozyme secreted from tear glands forms deposits on contact lenses. Which ingredient would be effective in a contact lens cleaner for removing these deposits? A ethanol B lysosomes C pH buffers D proteases
1 marks
Answer: D
38 Which feature of haemoglobin makes it a globular protein? A It has four cross-linked polypeptide chains forming a quaternary structure. B It has hydrophobic groups on the inside and hydrophilic groups on the outside. C It has hydrophobic interactions and is insoluble in water. D It has polypeptide chains which are cross-linked to form sheets.
1 marks
Answer: B
7 A peptide bond is formed between atoms of which two elements? A carbon and carbon B carbon and hydrogen C carbon and nitrogen D hydrogen and nitrogen
1 marks
Answer: C
8 Which features affect the tensile strength of collagen? 1 the helical structure of collagen chains 2 the small R group of the amino acids in collagen 3 the insoluble nature of collagen 4 the covalent bonds between collagen molecules A 1, 2, 3 and 4 B 1 and 3 only C 1, 2 and 4 only D 2, 3 and 4 only
1 marks
Answer: C
9 An amino acid can be represented as H R O N C C H H OH where R represents a variable side chain. Which is not a possible side chain? A CH3 B CH2CH2SCH3 C CH2CONH2 D HOCH2CH(OH)CH2OH
1 marks
Answer: D
8 Which set of statements correctly describes haemoglobin? A four polypeptide iron ions can in each chain, at 50 % saturation, chains, each associate with hydrophobic R two oxygen containing a oxygen forming groups of amino molecules are prosthetic group oxyhaemoglobin acids point towards transported by the the centre of the molecule molecule B polypeptide chains each chain contains two identical alpha each chain can interact to produce a a prosthetic group of chains and two transport an oxygen globular chain amino acids identical beta chains molecule surrounding an iron ion C polypeptide chains an iron ion is quaternary structure each molecule can interact to produce present within each of two alpha chains transport a total of an almost spherical haem group and two beta chains four oxygen atoms molecule D polypeptide chains iron ions in the in each chain, each molecule can produce a loose molecule can bind hydrophobic R transport a total of helical shape, which reversibly with groups of amino eight oxygen atoms curls to form a oxygen acids surround the spherical molecule iron ion
1 marks
Answer: A
10 Which rows show the chemical groups present in the biological molecules listed? biological presence of carboxyl presence of two or more molecule (COOH) groups hydroxyl (OH) groups 1 amino acid yes no 2 β-glucose no yes 3 glycerol no no 4 fatty acid yes no A 1, 2 and 3 B 1, 2 and 4 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: B
11 Which correctly matches the functional and structural features of cellulose, collagen, glycogen or triglyceride? structure molecule held function fibrous together by branched chains hydrogen bonds A cellulose support Jv Jv x triglyceride | energy source x x x B collagen strengthening Jv Jv x cellulose support v x v Cc collagen strengthening Jv Jv Jv glycogen storage x x v D glycogen storage x Jv Jv triglyceride | energy source x Jv x key /=true xX =false
1 marks
Answer: A
13 Which levels of protein structure can determine the specificity of an enzyme? 1 primary 2 secondary 3 tertiary 4 quaternary A 1, 2, 3 and 4 B 1, 2 and 3 only C 1, 2 and 4 only D 3 and 4 only
1 marks
Answer: A
8 At which levels of protein structure do ionic bonds occur? 1 secondary 2 tertiary 3 quaternary A 1 and 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: C
9 Myoglobin is a protein with a similar function to haemoglobin. However, myoglobin does not have a quaternary structure. Why does myoglobin not have a quaternary structure? A Myoglobin does not contain a haem group. B Myoglobin does not contain any alpha helices. C Myoglobin has a fibrous rather than a globular structure. D Myoglobin has only one polypeptide chain.
1 marks
Answer: D
10 The diagram shows the structure of the amino acid cysteine. H H H N H S C C C OH H H O When two of these amino acids join together what bond(s) are formed? A disulfide bonds only B disulfide and peptide bonds C hydrogen, disulfide and peptide bonds D peptide bonds only
1 marks
Answer: D
32 Which rows show the chemical groups present in the biological molecules listed? biological presence of carboxyl presence of two or more molecule (COOH) groups hydroxyl (OH) groups 1 amino acid yes no 2 β-glucose no yes 3 glycerol no no 4 fatty acid yes no A 1, 2 and 3 B 1, 2 and 4 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: B
35 Which correctly matches the functional and structural features of cellulose, collagen, glycogen or triglyceride? structure molecule held function fibrous together by branched chains hydrogen bonds A cellulose support J Jv x triglyceride | energy source x x x B collagen strengthening Jv Jv x cellulose support Jv x J Cc collagen strengthening Jv Jv Jv glycogen storage x x v D glycogen storage x Jv Jv triglyceride | energy source x Jv x key /=true xX = false
1 marks
Answer: A
36 Which set of statements correctly describes haemoglobin? A four polypeptide iron ions can in each chain, at 50 % saturation, chains, each associate with hydrophobic R two oxygen containing a oxygen forming groups of amino molecules are prosthetic group oxyhaemoglobin acids point towards transported by the the centre of the molecule molecule B polypeptide chains each chain contains two identical alpha each chain can interact to produce a a prosthetic group of chains and two transport an oxygen globular chain amino acids identical beta chains molecule surrounding an iron ion C polypeptide chains an iron ion is quaternary structure each molecule can interact to produce present within each of two alpha chains transport a total of an almost spherical haem group and two beta chains four oxygen atoms molecule D polypeptide chains iron ions in the in each chain, each molecule can produce a loose molecule can bind hydrophobic R transport a total of helical shape, which reversibly with groups of amino eight oxygen atoms curls to form a oxygen acids surround the spherical molecule iron ion
1 marks
Answer: A
7 Which is the strongest type of bonding found in proteins? A disulfide bonds B hydrogen bonds C hydrophobic interactions D ionic bonds
1 marks
Answer: A
20 Which is the strongest type of bonding found in proteins? A disulfide bonds B hydrogen bonds C hydrophobic interactions D ionic bonds
1 marks
Answer: A
10 Which level of protein structure maintains the globular shapes of enzymes? A primary B secondary C tertiary D quaternary
1 marks
Answer: C
11 Which substances contain carbon, hydrogen, oxygen and nitrogen? 1 collagen 2 amylopectin 3 deoxyribonucleic acid A 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: B
8 Which molecules contain C=O bonds? 1 amino acids 2 fatty acids 3 proteins A 1 and 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: D
15 Which substances contain carbon, hydrogen, oxygen and nitrogen? 1 collagen 2 amylopectin 3 deoxyribonucleic acid A 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: B
17 Which level of protein structure maintains the globular shapes of enzymes? A primary B secondary C tertiary D quaternary
1 marks
Answer: C
8 Which row is correct for each of the molecules? β-glucose collagen haemoglobin sucrose A hexose sugar structural contains the formed by with a molecular function, found in elements carbon, releasing a formula C6H12O6 tendons and hydrogen, iron, molecule of water blood vessel nitrogen and in a hydrolysis walls sulfur reaction B repeating a molecule each non-protein composed of two monomer of the consists of three haem group monosaccharides polysaccharide, polypeptide contains a central linked by a cellulose chains, each iron ion glycosidic bond containing a prosthetic group C monomer of the molecules lie has two identical formed by 1,6 glycosidic parallel to each α chains and two condensation of branches of the other, with cross- identical β chains two identical polysaccharide, links and monosaccharides glycogen staggered ends in its ring D polypeptide has all four levels digestion yields structure, the chains interact to of protein glucose and hydroxyl group of produce a fibrous structure and at fructose in equal carbon atom 1 is protein least four types of proportions above the plane bond of the ring
1 marks
Answer: D
12 Which molecules contain C=O bonds? 1 amino acids 2 fatty acids 3 glycerol A 1 and 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3
1 marks
Answer: A
9 Which molecules have a structural formula that contains C=O bonds? 1 glucose 2 glycerol 3 protein A 1 and 2 only B 1 and 3 only C 2 and 3 only D 1, 2 and 3 only
1 marks
Answer: B
10 Haemoglobin consists of two α chains and two β chains. Approximately 5 % of all humans have one amino acid in the β chain different from normal. Which level(s) of protein structure could be changed in these humans? A primary only B primary and quaternary only C primary, secondary and tertiary only D quaternary only
1 marks
Answer: C
12 Which row shows the types of bond found at different levels of protein structures? bonds level of protein structure peptide | hydrogen | ionic | hydrostatic A primary J x x v B secondary Xx v v x Cc tertiary x v v v D quaternary v x v v key Jv = present X = absent
1 marks
Answer: C
11 What describes a globular protein that is not soluble in water? A having amino acids with hydrophilic R groups facing out B having amino acids with polar R groups facing out C having a central core of amino acids with hydrophobic R groups D having amino acids with hydrophobic R groups facing out
1 marks
Answer: D
12 Features of four proteins, W, X, Y and Z, are described below. W consists of two polypeptides held together by disulfide bonds X consists of three polypeptides tightly coiled together Y consists of four polypeptides each with a prosthetic group Z consists of four polypeptides held together by disulfide bonds Which row correctly identifies the named proteins? antibody collagen haemoglobin A W X Y B W Y X C Z X Y D Z Y X
1 marks
Answer: C
7 The R groups (side chains) of amino acids can be hydrophobic, hydrophilic, acidic or basic. The diagram shows four different amino acid R groups. COOH NH2 OH CH3 CH2 (CH2)4 CH2 Ala Asp Lys Ser Which row is correct for these amino acid R groups? hydrophobic hydrophilic acidic basic A Ala Ser Asp Lys B Ala Ser Lys Asp C Asp Lys Ser Ala D Asp Ser Lys Ala
1 marks
Answer: A
11 Which molecules contain a carboxyl group? 1 amino acid 2 glycerol 3 saturated fatty acid 4 unsaturated fatty acid A 1 and 2 only B 3 and 4 only C 1, 3 and 4 only D 2, 3 and 4 only
1 marks
Answer: C
12 The diameter of some atoms when they form bonds are given in the table. single bond double bond atom / nm / nm H 0.060 – O 0.132 0.110 N 0.140 0.120 C 0.154 0.134 The approximate length of the amino acid shown below was estimated using the figures in the table. R O H N C C O H H H 0.7 nm What would be the approximate length of a dipeptide formed using this amino acid? A 0.9 nm B 1.2 nm C 1.4 nm D 1.7 nm
1 marks
Answer: B
7 Two solutions, 1 and 2, one containing starch and sucrose, and the other containing glucose and protein, were tested with a variety of reagents to confirm their identity. The table shows the conclusions from the results recorded for the various tests. Which row identifies the two solutions? boil with boil with add iodine Benedict’s add biuret Benedict’s solution solution after solution solution acid hydrolysis 1 2 1 2 1 2 1 2 key A + – + – – + – + + = biological molecule present B – + + – + – – + – = biological C + – – + + – – + molecule absent D – + + – + + + –
1 marks
Answer: C
12 What occurs during protein denaturation by extremes of pH? 1 breakage of peptide bonds leading to loss of shape of active site 2 disruption of existing ionic bonds between amino acid R-groups 3 loss of α-helical regular arrangement of amino acids 4 loss of protein tertiary structure resulting in loss of function A 1, 2, 3 and 4 B 2, 3 and 4 only C 1 and 3 only D 2 and 4 only
1 marks
Answer: B
8 Collagen is a macromolecule with three polypeptides lying closely side by side in the form of a triple helix. Every third amino acid in each polypeptide has the shortest possible R-group or side chain (– H) to allow close packing of the polypeptides. Which is the amino acid? A glucose B glycerol C glycine D guanine
1 marks
Answer: C
9 The diagrams show the structures of two amino acids, each of which has two amine (–NH2) groups. 1 2 4 5 H2N CH COOH H2N CH COOH CH2 CH2 3 C CH2 O NH2 6 C O NH2 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 4 B 1 and 5 C 2 and 6 D 3 and 5
1 marks
Answer: B
10 Each list, 1, 2 and 3, shows some substances found in animal tissues. 1 glucose, cholesterol, triglycerides, water. 2 glycogen, antibodies, adenine, phospholipids. 3 haemoglobin, carbon dioxide, mRNA, monosaccharides. Which shows one or more substances that contain nitrogen atoms? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: D
38 A student wrote down three statements about antibodies. 1 Their structure depends on peptide, hydrogen and disulfide bonds. 2 They are protein molecules with both tertiary and quaternary structure. 3 Four polypeptides provide four antigen binding sites. Which statements are true? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: B
8 The formation of glycosidic and peptide bonds is responsible for polymerisation in some biological molecules. Which bonds are found in which molecules? glycosidic peptide A glycerol glycoprotein B glycogen glycerol C glycogen glycoprotein D glycoprotein glycolipid
1 marks
Answer: C
9 The diagrams show the structures of two amino acids, each of which has more than one amine (–NH2) group. 1 2 4 H2N CH COOH H2N CH COOH CH2 CH2 CH2 CH2 C 3 CH2 O NH2 NH 5 C HN NH2 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 4 B 2 and 4 C 2 and 5 D 3 and 4
1 marks
Answer: A
10 Which explains why haemoglobin is able to carry oxygen? A It consists of four polypeptides. B It contains iron. C It has a quaternary structure. D It is a globular protein.
1 marks
Answer: B
9 The diagrams show the structures of two amino acids, each of which has more than one amine (–NH2) group. 1 3 4 H2N CH COOH H2N CH COOH CH2 CH2 CH2 C 5 O NH2 CH2 NH 2 C HN NH2 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 3 B 1 and 5 C 2 and 4 D 2 and 5
1 marks
Answer: A
10 Which combination of bond types correctly shows the weak and strong bonds that hold a molecule of protein in shape? types of bond hydrogen disulfide ionic A strong strong weak B strong weak strong C weak strong strong D weak strong weak
1 marks
Answer: D
10 The diagram shows the structure of four amino acids in solution. COO– COO– H C H3N+ CH2 CH2 CH2 CH2 C N+H3 N+H3 H H glycine lysine COO– O COO– CH3 C C CH2 C N+H3 O– N+H3 H H alanine aspartate Which of these four amino acids have an overall charge? A alanine and aspartate B alanine and glycine C aspartate and lysine D glycine and lysine
1 marks
Answer: C
11 Which level of organisation of a haemoglobin molecule is coded by a DNA molecule? A primary structure B secondary structure C tertiary structure D quaternary structure
1 marks
Answer: A
11 Which molecule contains a glycosidic bond? A B H H O OH HO CH2 C C H C O C R H O O N CH3 CH2 C C H H C O C R H O O N CH3 C C H H C O C R O N H H H C D H CH2OH N O N H O H C H C O CH2OH H O C C C C H N C C C C H C N H N O OH H O H OH CH2OH HO N C C N C C C C O H N H OH OH H H
1 marks
Answer: C
12 The diagrams show the structures of two amino acids, each of which has two carboxylic acid (–COOH) groups. 1 3 4 H2N CH COOH H2N CH COOH CH2 CH2 COOH 2 CH2 COOH 5 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 4 B 1 and 5 C 2 and 3 D 2 and 5
1 marks
Answer: A
21 What is the correct sequence for the processes involved in the formation of an enzyme in a cell? A transcription → condensation → translation → ionic bonding B translation → hydrogen bonding → transcription → condensation C transcription → translation → condensation → ionic bonding D translation → transcription → ionic bonding → hydrogen bonding
1 marks
Answer: C
9 Which comparative statements concerning biological molecules are correct? 1 A collagen molecule is a fibrous protein that contains many amino acids with hydrophobic R-groups whereas a haemoglobin molecule is a globular protein with no amino acids with hydrophobic R-groups. 2 Sucrose hydrolysis results in glycosidic bond breakage and the production of equal proportions of fructose and α-glucose molecules, whereas cellulose hydrolysis results in only β-glucose molecules. 3 The glycosidic bonds of glycogen have been formed between two α-glucose molecules, whereas with amylopectin, the bonds have been formed between an α-glucose molecule and a β-glucose molecule. A 1 and 2 B 1 and 3 C 2 only D 3 only
1 marks
Answer: C
11 The diagram represents an amino acid. H R O N C C H H OH R represents a variable side chain. Which is not a possible side chain? A CH3 B CH2CH2SCH3 C CH2CONH2 D HOCH2CH(OH)CH2OH
1 marks
Answer: D
16 One type of antigen is formed by a reaction between two different molecules. Apart from oxygen, which other elements are found in this antigen? A carbon and hydrogen only B hydrogen and nitrogen only C carbon, nitrogen and phosphorus D carbon, hydrogen, nitrogen and sulfur
1 marks
Answer: D
40 The growth of crop plants is often limited by the availability of nitrogen in the soil. The graph shows the results of an investigation into the yield of a crop plant, with increasing levels of nitrogen supplied. 7 6 5 yield of a crop plant 4 / tonnes per ha 3 2 1 0 0 40 80 120 160 nitrogen supplied / kg per ha Which of the following best explains the shape of this curve? protein synthesis DNA synthesis A increases no effect B no effect no effect C increases increases D no effect increases
1 marks
Answer: C
8 Which correctly matches the functional and structural features of cellulose, collagen, glycogen or triglyceride? structure molecule held function fibrous together by branched chains hydrogen bonds A cellulose support J Jv x triglyceride | energy source x x x B collagen strengthening Jv Jv x cellulose support v x J Cc collagen strengthening Jv Jv Jv glycogen storage x x v D glycogen storage x Jv Jv triglyceride | energy source x Jv x key /=true xX = false
1 marks
Answer: A
9 The diagram shows the relationship between the levels of protein structure and bonds. 1 2 3 4 5 Which row is correct? 1 2 3 4 5 A primary peptide secondary ionic tertiary B secondary hydrogen tertiary peptide primary C tertiary ionic primary peptide quaternary D quaternary ionic tertiary ionic secondary
1 marks
Answer: D
10 Which of the bonds stabilising the tertiary structure of a protein would be least likely to break when the temperature is increased above the optimum for the protein? A disulfide B hydrogen C hydrophobic D ionic
1 marks
Answer: A
11 The diagram shows the structure of four amino acids in solution. COO– COO– H C H3N+ CH2 CH2 CH2 CH2 C NH3 + NH3 + H H glycine lysine COO– O COO– CH3 C C CH2 C NH3 + O– NH3 + H H alanine aspartate Which amino acids have no overall charge? A alanine and aspartate B alanine and glycine C aspartate and lysine D glycine and lysine
1 marks
Answer: B
13 Which words from the table correctly complete the paragraph about enzymes? When the pH of an environment is decreased below an enzyme’s optimum pH, ……1…… bonds between adjacent ……2…… groups, holding the ……3…… structure, are disrupted. 1 2 3 A hydrogen and ionic R tertiary B hydrogen hydroxyl secondary C ionic and peptide R primary and tertiary D peptide amine primary
1 marks
Answer: A
18 The enzyme lactase is found in the membranes of epithelial cells lining the small intestine. The enzyme is formed by a single polypeptide that folds to give three regions. • an active site with the free amino group outside the cell • a short section inside the membrane • a short section inside the cell What type of amino acid would be found in each of the three regions? inside the inside the outside cell membrane cell A hydrophilic hydrophobic hydrophilic B hydrophilic hydrophobic hydrophobic C hydrophobic hydrophilic hydrophobic D hydrophobic hydrophobic hydrophilic
1 marks
Answer: A
10 Which of the following terms can be used to describe the secondary structure of a protein? 1 dipeptide 2 specific order of amino acids 3 α-helix 4 fibrous structure 5 β-pleated sheet A 1, 3, 4 and 5 B 1, 2 and 4 C 2 and 4 only D 3 and 5 only
1 marks
Answer: D
11 Why is haemoglobin stated to have a quaternary structure? A It has four haem groups. B It has two or more polypeptide chains. C It is coiled into a precise shape. D It is held together by four types of bonds.
1 marks
Answer: B
8 The diagrams show different types of bond found in biological molecules. 1 2 3 O NH O CH2 S S CH2 C N H 4 5 NH2 + O– O C CH2 C C CH2 C C O O C O C Which combination of bonds could not be found in a protein with a tertiary structure? A 1, 2, 3 and 4 B 1, 2 and 4 only C 3 and 5 D 5 only
1 marks
Answer: D
11 Which description is correct? A A collagen molecule has a high proportion of the amino acid glycine, which has a very small side chain. B A group of three collagen fibres forms a strong, insoluble coiled structure termed a triple helix. C Each of the collagen polypeptides in a collagen molecule has a regular spiral arrangement of many alpha helices. D Peptide bonds are present between amino acids of the same polypeptide and between the different polypeptides forming the collagen molecule.
1 marks
Answer: A
7 Which type of bond holds together an α-helix or β-pleated sheet of a protein? A disulfide B hydrogen C ionic D peptide
1 marks
Answer: B
8 What describes only the quaternary structure of haemoglobin? 1 α-helix 2 a dipeptide 3 a globular structure 4 the specific order of amino acids 5 four polypeptide chains joined together A 1, 2 and 3 B 2, 4 and 5 C 1 and 4 D 5 only
1 marks
Answer: D
21 In a ribosome, which bond holds together two adjacent amino acids? A disulfide B hydrogen C ionic D peptide
1 marks
Answer: D
8 The diagram shows the three dimensional structure of collagen. Which labelled part represents a molecule of collagen? C B D A
1 marks
Answer: C
9 Which type of bond does not hold together the tertiary structure of a protein? A disulfide B hydrogen C hydrophobic interactions D peptide
1 marks
Answer: D
11 The protein glutenin gives bread dough its elasticity. The diagram represents a polypeptide of glutenin. tightly tightly coiled coiled region region loose spiral What describes the structure of glutenin? A quaternary structure because there are both globular and fibrous regions B quaternary structure because there are both spiral and tightly coiled regions C secondary structure because the loose spiral is an α-helix D tertiary structure because the different regions form a 3D shape
1 marks
Answer: D
10 The diagrams show the amino acid serine. Which circled area is different in all other amino acids? A B H H H H N H N H HO C C C OH HO C C C OH O H H O H H C D H H H H N H N H HO C C C OH HO C C C OH O H H O H H
1 marks
Answer: C
8 The synthesis of biological molecules requires the formation of bonds. Which row is correct? a bond forms between a β-1,4 bond forms the hydroxyl group of the carboxylic the phosphate of one between the monomers acid group is removed and a monomer and the sugar to give an unbranched carbon-nitrogen bond is formed to of the next monomer chain give an unbranched chain A polynucleotide amylose polypeptide B polynucleotide cellulose polypeptide C phospholipid amylose polynucleotide D phospholipid cellulose polynucleotide
1 marks
Answer: B
10 High concentrations of urea break all bonds, except covalent bonds, in protein molecules. Which level of protein structure would remain unchanged when a protein is treated with urea? A primary B secondary C tertiary D quaternary
1 marks
Answer: A
11 Haemoglobin, a globular protein, consists of four polypeptide chains, two alpha chains and two beta chains. In normal individuals, in the DNA which codes for each beta chain, the sixth triplet has a code for glutamic acid. In individuals with sickle cell anaemia this base triplet mutates and codes for valine. What does this mutation change in the haemoglobin molecule? A the iron content B the primary structure C the quaternary structure D the secondary structure
1 marks
Answer: B
10 When proteins are mixed with some organic solvents, hydrophobic interactions and hydrogen bonding are changed in the protein molecules. Which levels of protein structure would be affected? 0 0O WwW D> level of protein structure secondary tertiary << x quaternary S44 key J = affected X = not affected
1 marks
Answer: D
10 The diagrams show the structures of two amino acids, one of which has two amine (–NH2) groups and the other has two carboxylic (–COOH) groups. 1 3 H2N CH COOH H2N CH COOH CH2 CH2 CH2 CH2 CH2 COOH 4 NH C 2 HN NH2 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 3 B 2 and 3 C 2 and 4 D 4 and 1
1 marks
Answer: A
11 Proteins which transport sugars out of cells have been identified. These proteins are called SWEETs. Each SWEET has seven coiled, cylindrical regions which together make up a pore through the cell surface membrane bilayer, as shown in the diagram. 1 2 3 7 4 6 5 What describes each of the seven coiled regions (1-7) of a SWEET shown in the diagram? A primary structure held in its shape by bonds such as hydrogen bonds B primary structure held in its shape by peptide bonds C secondary structure held in its shape by bonds such as hydrogen bonds D secondary structure held in its shape by peptide bonds
1 marks
Answer: C
6 Which biological molecules always contain the element nitrogen? A amino acids, cellulose, mRNA B amino acids, DNA, lipids C enzymes, mRNA, tRNA D membrane proteins, starch, tRNA
1 marks
Answer: C
7 Which statement about the quaternary structure of proteins is correct? A consists of four subunits B depends on the presence of metal ions C depends on the primary structure of the subunits D is made of α and β subunits
1 marks
Answer: C
8 Which set of statements correctly describes haemoglobin? A in each chain, at 50 % saturation, four polypeptide iron ions can hydrophobic R two oxygen chains, each associate with groups of amino molecules are containing a haem oxygen forming acids point towards transported by the group oxyhaemoglobin the centre of the molecule molecule B each chain contains consists of two polypeptide chains a haem group of each chain can identical alpha interact to produce a amino acids transport an oxygen chains and two globular chain surrounding an iron molecule identical beta chains ion C polypeptide chains quaternary structure an iron ion is each molecule can interact to produce has two alpha present within each transport a total of an almost spherical chains and two beta haem group four oxygen atoms molecule chains D polypeptide chains in each chain, iron ions in the produce a loose hydrophobic R each molecule can molecule can bind helical shape, which groups of amino transport a total of reversibly with folds to form a acids surround the eight oxygen atoms oxygen spherical molecule iron ion
1 marks
Answer: A
9 The diagrams show different types of bond found in biological molecules. 1 2 3 O NH O C CH2 S S CH2 C N H 4 5 NH3 + O– O C C C CH2 C C CH2 C O C O O Which bonds are found in proteins with a tertiary structure? A 1, 2, 3 and 4 B 2, 3, 4 and 5 C 1 and 5 D 2 and 4 only
1 marks
Answer: A
10 Which of the bonds will be last to break as the temperature of an enzyme is increased? A hydrogen B hydrophobic interactions C ionic D peptide
1 marks
11 What could describe the tertiary structure of a protein? 1 α-helix 2 a globular structure 3 the specific order of amino acids 4 a specific three-dimensional (3D) shape A 1, 2 and 3 B 1, 2 and 4 C 2 and 4 only D 3 and 4
1 marks
Answer: C
7 Which row is correct for each of the molecules? collagen haemoglobin sucrose A has a structural contains the formed by function, found in elements carbon, releasing a blood vessel hydrogen, iron, molecule of water walls nitrogen and in a hydrolysis sulfur reaction B molecules consist each non-protein composed of two of three haem group monosaccharides polypeptide contains a central linked by a chains, linked by iron ion glycosidic bond ionic bonds C molecules lie has two identical formed by parallel to each α chains and two condensation of other, with cross- identical β chains two identical links and monosaccharides staggered ends D polypeptide has all four levels digestion yields chains interact to of protein glucose and produce a fibrous structure and at fructose in equal protein least four types of proportions bond
1 marks
Answer: D
9 Threonylvaline is a dipeptide formed from the two amino acids, threonine and valine. A peptide bond forms between the carboxyl group of threonine and the amine group of valine. The side-chains (R groups) of the two amino acids are shown. HO CH3 H3C CH3 CH CH threonine valine Which molecular structure is threonylvaline? A B HO CH3 H3C CH3 HO CH3 H3C CH3 CH O CH CH H CH H O H O N C C N C C N C C O N C C H H H H OH H H H H H OH C D H3C CH3 HO CH3 HO CH3 H3C CH3 CH O CH CH CH H O H O N C C N C C N C C N C C H H H H OH H O H H H OH
1 marks
Answer: A
10 Which feature explains why haemoglobin is soluble? A All four polypeptide chains are linked together to form a spherical molecule. B Each polypeptide chain folds due to interactions between hydrophobic R groups. C The hydrophilic R groups are arranged around the outside of the molecule. D The iron-containing haem group of each polypeptide chain is water soluble.
1 marks
Answer: C
10 Some of the molecules found in animal tissues are grouped into three lists. 1 glucose, cholesterol, triglycerides, water 2 glycogen, antibodies, adenine, phospholipids 3 haemoglobin, carbon dioxide, mRNA, monosaccharides Which lists include one or more molecules that always contain nitrogen atoms? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: D
11 Haemoglobin consists of two α chains and two β chains. Approximately 5% of all humans have one amino acid in the β chain that has been changed, affecting the structure and stability of haemoglobin. Which of the levels of protein structure could be changed in the haemoglobin of these humans? A primary only B primary and quaternary only C primary, secondary, tertiary and quaternary D secondary, tertiary and quaternary only
1 marks
Answer: C
12 Which row gives the correct description of both a collagen molecule and a collagen fibre? collagen molecule collagen fibre A α and β polypeptide chains molecules of collagen forming a double helix, held arranged randomly to each other, together by disulfide bonds linked by hydrogen bonds B a polypeptide chain, with repeating three molecules of collagen, amino acids, forming an α-helix forming a triple helix, held together by hydrogen bonds C a polypeptide chain, with three α helical collagen three repeating amino acids, molecules, forming a triple helix, forming a helix held together by ionic bonds D three helical polypeptide chains, molecules of collagen lying forming a triple helix, held parallel and cross-linked to each together by hydrogen bonds other
1 marks
Answer: D
13 The diagrams show the structures of two amino acids, each of which has two amine (–NH2) groups. 1 2 4 5 H2N CH COOH H2N CH COOH CH2 CH2 3 C CH2 O NH2 6 C O NH2 A peptide bond is formed between the two amino acids. Which groups could form the peptide bond? A 1 and 4 B 1 and 5 C 2 and 6 D 3 and 5
1 marks
Answer: B
11 The diagram shows the molecular structure of a peptide. O NH2 C CH2 H O CH3 H H C N C C OH N C C N C H H H O CH2 H O OH Which molecules would result from the complete hydrolysis of the peptide? O NH2 C CH2 H CH2 H H H CH3 A N C COOH N C COOH N C COOH H H H H CH2 H O NH2 OH C H CH2 H H H CH3 B N C COOH N C COOH N C COOH H H H H H C OH H CH3 O NH2 C H CH2 H H H CH3 C N C COOH N C COOH N C COOH H H H H CH2 H NH2 OH O C H CH2 H H H H D N C COOH N C COOH N C COOH H H H H CH2 H OH
1 marks
Answer: C
12 The diagram shows a haemoglobin molecule. β-globin chain 3 α-globin chain 4 2 α-globin chain β-globin chain 1 Which row identifies the different parts of the molecule? 1 2 3 4 α-helix β-pleated binding site hydrophobic A sheet amino acids binding site hydrophilic α-helix hydrophobic B amino acids amino acids haem hydrophobic α-helix hydrophilic C group amino acids amino acids hydrophobic β-pleated haem binding site D amino acids sheet atom
1 marks
Answer: B
5 Boiling the bones and teeth from dead animals can be used to produce a type of glue. The glue is formed from the collagen fibres present in bones and teeth. Which statement describes the changes to collagen that occur when the glue is produced? A The fibres of collagen become more coiled. B The fibres of collagen become more flexible. C The helices of collagen molecules unwind. D The molecules of collagen dissolve in water.
1 marks
Answer: C
6 What describes the primary structure of a protein? A α-helix B a dipeptide C a globular structure D the specific order of amino acids
1 marks
Answer: D
7 The diagram shows some of the relationships between cellulose, collagen and haemoglobin. 1 2 3 4 5 Which row is correct? 1 2 3 4 5 A cellulose carbohydrate collagen protein haemoglobin B cellulose fibrous haemoglobin structural collagen C haemoglobin globular cellulose carbohydrate collagen D haemoglobin protein collagen structural cellulose
1 marks
Answer: D
8 The diagram shows a protein molecule. globular head key long polypeptide short polypeptide Two long polypeptides each form α-helices for much of their length and these twist together into a fibre. At one end, each of these polypeptides coils into a globular head. Two short polypeptides bind to each head. What describes the protein structure of this molecule? A quaternary structure because each molecule consists of six polypeptides B secondary structure because the long polypeptides form α-helices C tertiary structure because the α-helices form a fibre D tertiary structure because the heads form globular proteins
1 marks
Answer: A
7 A student carried out four tests for biological molecules on a sample of milk. The tests and their results were as follows. ● Heating to 80 °C with Benedict’s solution gave a brick red colour. ● Adding Biuret solution gave a purple colour. ● Adding iodine solution gave an orange colour. ● Boiling with acid, followed by neutralisation, then heating to 80 °C with Benedict’s solution gave a brick red colour. Which biological molecules must be present in the milk? 1 non-reducing sugars 2 protein 3 reducing sugars 4 starch A 1, 2 and 3 B 1 and 2 only C 2 and 3 only D 3 and 4
1 marks
Answer: C
11 Which row correctly matches the functional and structural features of cellulose, collagen, glycogen or triglyceride? structure molecules held molecule function fibrous together by branched chains hydrogen bonds A cellulose support Jv Jv x triglyceride energy source x x x B collagen strengthening Jv Jv x cellulose support Jv x Jv Cc collagen strengthening Jv Jv Jv glycogen storage x x Jv D glycogen storage x Jv Jv triglyceride | energy source x Jv x key J=true X = false
1 marks
Answer: A
12 A polypeptide has a number of amino acids (n). How many peptide bonds and R groups (side chains) does this polypeptide have? A n – 1 peptide bonds and n – 1 R groups B n – 1 peptide bonds and n R groups C n peptide bonds and n – 1 R groups D n peptide bonds and n R groups
1 marks
Answer: B
9 The diagram shows the amino acids in a polypeptide. key type of amino acid polar basic polar acidic Asp Arg Lys polar Cys Thr Lys Leu non-polar Pro Asn Arg Val Ser Asn Glu Lys Thr Arg Phe Met Lys Phe Gln Met Ala His Val Gln Met Ala His Asn Asp Ala Glu Cys Thr Ser C terminal end Tyr Ser Glu Asn Lys Ser Thr Ser Ser N terminal end Ser Ala Ala An enzyme catalyses the hydrolysis of any peptide bond between a non-polar amino acid and any polar amino acid. How many small peptides and single amino acids will be formed by the action of this enzyme? small single peptides amino acids A 6 1 B 8 1 C 12 3 D 13 4
1 marks
Answer: D
10 A person with diabetes is unable to make enough of the protein insulin. Some forms of diabetes can be treated by using insulin produced by animals. Scientists have compared the amino acids in insulin produced by animals to human insulin. Which level of protein structure were the scientists studying? A primary B secondary C tertiary D quaternary
1 marks
Answer: A
12 Which levels of protein structure are maintained by disulfide bonds? A secondary, tertiary and quaternary B tertiary and quaternary only C quaternary only D tertiary only
1 marks
Answer: B
9 Which diagram correctly shows the formation of a peptide bond between two amino acids? A B H H O H H O H H O N C C N C C N C C H2O H H C H OH H H OH H H OH H H O H C H H2O N C C C OH H H O OH C D H H O H H O N C C N C C H H C H OH H H C H OH H H O H H O C N C C C O OH N C C N O H H OH H H H2O H H OH H2O
1 marks
Answer: A
11 Which molecules are globular proteins? 1 amylase 2 haemoglobin 3 DNA polymerase A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 only
1 marks
Answer: A
12 When hydrolysed, which molecules have products containing a carboxyl group? 1 phospholipids 2 polysaccharides 3 proteins A 1 and 2 B 1 and 3 C 2 and 3 D 3 only
1 marks
Answer: B
7 The diagram shows relationships between some important molecules and bonds. 1 peptide glycosidic 3 ester 2 triglyceride cellulose vegetable oil amylopectin What is represented by circles numbered 1, 2 and 3? 1 2 3 A bonds formed carbohydrates lipids by condensation B bonds formed lipids carbohydrates by condensation C bonds formed carbohydrates lipids by hydrolysis D bonds formed lipids carbohydrates by hydrolysis
1 marks
Answer: A
10 The diagrams show two arrangements of amino acids in a protein. T S Which row correctly names the bonds at S or T? ionic bond hydrogen bond A absent S and T B S only T only C S and T absent D T only S and T
1 marks
Answer: A
11 Students were asked to highlight only the R groups of two ring-shaped amino acids. Which pair of diagrams are correct for both amino acids? H O H O H3N+ C C H2N+ C C A O– O– C NH H2C CH2 C CH2 C NH+ H O H O H3N+ C C H2N+ C C B O– O– C NH H2C CH2 C CH2 C NH+ H O H O H3N+ C C H2N+ C C C O– O– C NH H2C CH2 C CH2 C NH+ H O H O H3N+ C C H2N+ C C D O– O– C NH H2C CH2 C CH2 C NH+
1 marks
Answer: D
12 Which words from the table correctly complete the paragraph about enzymes? When the pH of an environment is decreased below the optimum pH of an enzyme, ««1«« bonds between adjacent ««2«« groups, holding the ««3«« structure, are disrupted. 1 2 3 A hydrogen and ionic R tertiary B hydrogen hydroxyl secondary C ionic and peptide R primary and tertiary D peptide amine primary
1 marks
Answer: A
8 The diagram shows the relationship between some biological molecules. 1 2 3 4 5 Which row is correct? 1 2 3 4 5 A α-glucose carbohydrate sucrose monomer fructose B cellulose polymer starch carbohydrate amylase C fructose reducing sugar β-glucose monomer amino acid D haemoglobin protein amylose polymer cellulose
1 marks
Answer: C
10 Which molecules contain C=O bonds? 1 amino acids 2 fatty acids 3 glycerol A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: B
11 Which row describes a collagen molecule? bonds stabilising properties primary structure helix the molecule A disulfide high temperatures high proportion double increase flexibility of glycine B disulfide resistant to repeat sequences single stretching of three amino acids C hydrogen high tensile repeat sequences triple strength of three amino acids D hydrogen insoluble high proportion alpha in water of glycine and proline
1 marks
Answer: C
9 Which molecules contain the following bonds? ester hydrogen disulfide A amylase haemoglobin catalase B glycerol glycogen collagen C lipids amylopectin amylose D phospholipids cellulose antibodies
1 marks
Answer: D
11 Which description is correct for collagen? A A collagen molecule has a high proportion of the amino acid glycine, which has a very small R group. B A group of three collagen fibres forms a strong, insoluble coiled structure termed a triple helix. C Each of the collagen polypeptides in a collagen molecule has a regular spiral arrangement of many alpha helices. D Peptide bonds are present between amino acids of the different polypeptides forming the collagen molecule.
1 marks
Answer: A
11 Which statements about a peptide bond are correct? 1 It joins two monomers which are always identical to each other. 2 It contains four different atoms. 3 It can be broken by the addition of water at room temperature. 4 It is important in the primary structure of proteins. A 1, 2 and 3 B 1 and 3 only C 2, 3 and 4 D 2 and 4 only
1 marks
Answer: D
12 Which statements about the primary structure of a protein are correct? 1 It may be branched. 2 It is determined by the sequence of DNA bases. 3 It is unique to that protein. 4 It determines the tertiary structure of the protein. A 1, 2 and 3 B 1, 2 and 4 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: D
15 The diagram shows a glycoprotein embedded in the cell surface membrane of a human red blood cell. This glycoprotein is part of a system of cell surface blood group recognition sites. key = carbohydrate P cell surface membrane Q Which row identifies the role of this glycoprotein and regions P and Q of the molecule? role of region P region Q glycoprotein A antigen amino acids with amino acids with hydrophilic hydrophobic R groups R groups in the cell’s cytoplasm B carrier amino acids with amino acids with hydrophilic hydrophilic R groups R groups in the cell’s cytoplasm C channel amino acids with amino acids with hydrophobic hydrophilic R groups R groups outside the cell D receptor amino acids with amino acids with hydrophobic hydrophobic R groups R groups outside the cell
1 marks
Answer: A
10 Which diagram shows where a peptide bond would be formed? A B H R O H R O H R O O R H N C C N C C N C C C C N H H OH H H OH H H OH H O H H C D H R O H R O H R O H H N C C N C C N C C N H H OH H H OH H H OH H C R C O OH
1 marks
Answer: A
11 Which statements about collagen molecules are correct? 1 Both types of secondary structure occur within the molecules. 2 Large numbers of hydrogen bonds stabilise the molecules. 3 Repeated amino acid sequences determine the tertiary structure. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: D
12 The protein glutenin gives bread dough its elasticity. The diagram represents a polypeptide of glutenin. tightly tightly coiled coiled region region loose spiral What describes the structure of glutenin? A quaternary structure because there are both globular and fibrous regions B quaternary structure because there are both spiral and tightly coiled regions C secondary structure because the loose spiral is an α-helix D tertiary structure because the different regions form a 3D shape
1 marks
Answer: D
12 The table shows the diameter of some atoms when they form bonds. single bond double bond atom / nm / nm H 0.060 – O 0.132 0.110 N 0.140 0.120 C 0.154 0.134 The approximate length of the amino acid shown was estimated using the figures in the table. R O H N C C O H H H 0.7 nm What would be the approximate length of a dipeptide formed using this amino acid? A 0.9 nm B 1.2 nm C 1.4 nm D 1.7 nm
1 marks
Answer: B
14 Some animals produce antimicrobial proteins which protect them from pathogens. These proteins could be used to kill human pathogens, however when used as a medicine they are broken down by protein-digesting enzymes. Replacing one of the amino acids found in the protein with one that had been synthesised in the laboratory resulted in a modified protein that was not broken down. What could explain why this modified protein was not broken down by the protein digesting enzymes? 1 The modified protein has a different tertiary structure to the original protein. 2 The modified protein is not complementary in shape to the enzyme’s active site. 3 The modified protein is unable to induce a fit with the protein digesting enzyme. A 1, 2 and 3 B 1 and 2 only C 2 and 3 only D 2 only
1 marks
Answer: A
11 The table compares three molecules, X, Y and Z, which contain the elements carbon, hydrogen and oxygen only. The percentage of carbon, hydrogen and oxygen atoms in each molecule is shown. molecule % carbon % hydrogen % oxygen X 25.0 50.0 25.0 Y 28.5 47.7 23.8 Z 34.6 61.6 3.8 Which row correctly identifies molecules X, Y and Z? molecule X Y Z A monosaccharide disaccharide polysaccharide B monosaccharide polysaccharide triglyceride C polysaccharide triglyceride monosaccharide D triglyceride monosaccharide polysaccharide
1 marks
Answer: B
14 Which levels of protein structure can determine the specificity of an enzyme? 1 primary 2 secondary 3 tertiary 4 quaternary A 1, 2, 3 and 4 B 1, 2 and 3 only C 1, 2 and 4 only D 3 and 4 only
1 marks
Answer: A
12 What is the minimum number of carbon atoms in an amino acid? A 1 B 2 C 3 D 4
1 marks
Answer: B
7 Which diagram shows the formation of a peptide bond? A B H H O H H O H H O O H H N C C N C C N C C C C N H H OH H H OH H H OH HO H H H2O H2O C D H H O H H O H H O O H H N C C N C C N C C C C N H H OH H H OH H H OH HO H H H2O H2O
1 marks
Answer: A
8 In enzyme-catalysed reactions, the position of the amino acids found at the active site is important. During the synthesis of enzymes, amino acids are brought together in the correct position to form the active site. Which levels of protein structure must be involved in forming the active site? level of protein structure primary | secondary tertiary quaternary v v v v key J = involved X = not involved 0 OO WwW PY x « & S44 x KOK \ <x
1 marks
Answer: B
9 Which features affect the tensile strength of collagen? 1 the helical structure of collagen chains 2 the small R group of the amino acids in collagen 3 the insoluble nature of collagen 4 the bonds between collagen molecules A 1, 2, 3 and 4 B 1, 2 and 4 only C 1 and 3 only D 2, 3 and 4 only
1 marks
Answer: B
13 Which features of collagen result in it having high tensile strength? 1 Bonds form between adjacent molecules. 2 Each three-stranded molecule is held together by hydrogen bonds. 3 Every third amino acid in the polypeptide is small. 4 The primary structure is held together by peptide bonds. A 1, 2 and 3 B 1, 3 and 4 C 1 and 2 only D 2, 3 and 4
1 marks
Answer: A
14 Which levels of protein structure would always be changed if an enzyme works by the induced fit hypothesis? primary secondary tertiary quaternary v v v v key ¥ = always changed 0 0O WwW D> v v x x Jv x X = not changed x x x < « x
1 marks
Answer: D
12 Which statements could be used to describe enzyme molecules and antibody molecules? 1 Hydrogen bonds stabilise the structure of the protein and are important for it to function efficiently. 2 Hydrophilic R-groups point in to the centre of the molecule and cause it to curl into a spherical shape. 3 The tertiary structure of the protein molecule plays an important role in the functioning of the protein. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: C
9 Which rows show the chemical groups present in the biological molecules listed? biological presence of carboxyl presence of two or more molecule (COOH) groups hydroxyl (OH) groups 1 amino acid yes no 2 β-glucose no yes 3 glycerol no no 4 fatty acid yes no A 1, 2 and 3 B 1, 2 and 4 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: B
11 Fibrous proteins are composed of chains of amino acids held together by bonds. An example of part of a fibrous protein is shown. O R H N N H O X Y O R H N N H O Which type of bond is at X and Y? X Y A disulfide hydrophobic interaction B hydrogen peptide C hydrophobic interaction ionic D ionic peptide
1 marks
Answer: B
12 Which row about the structure of proteins is correct? primary structure secondary structure quaternary structure A is the number is the left-handed is the sub-unit of amino acids spiral formed by the polypeptides that present in a protein primary structure link together to form a protein B is the order of is the coiling of a contains two types amino acids present in chain of amino acids of polypeptide that a protein to form a β-pleated interact forming the encoded by DNA sheet or α-helix shape of a protein C is the result of occurs because of is formed by four translation of an attraction between polypeptides and mRNA molecule by hydrogen and an additional reactive a ribosome into a oxygen atoms in group attached to the chain of amino acids the peptide bonds protein D is the sequence is formed by is formed by the of amino acids in hydrogen bonding linking together a protein coded by between amino acids of more than one an mRNA molecule forming the polypeptide to primary structure form a protein
1 marks
Answer: D
9 Three proteins that have a quaternary structure are listed. • Type IX collagen is formed from three different polymers. • The main form of haemoglobin contains two alpha globins and two beta globins. • HIV protease consists of two identical polymers. Which row shows the correct number of genes needed to code for each protein? number of genes type IX HIV haemoglobin collagen protease A 1 2 2 B 1 4 1 C 3 2 1 D 3 4 2
1 marks
Answer: C
10 The diagrams show the structure of an amino acid with some parts of the molecule shaded. Which diagram shows the shaded part of the molecule that is common to all amino acids? A B H H C C NH2 NH2 CH3 CH3 COOH COOH C D H H C C NH2 NH2 CH3 CH3 COOH COOH
1 marks
Answer: B
11 The diagrams show three examples of different bonds. bond 1 bond 2 bond 3 O NH O C C N CH2 S S CH2 H Which bonds hold the secondary structure of proteins together? A 1, 2 and 3 B 1 and 2 only C 1 only D 2 and 3 only
1 marks
Answer: C
9 Which molecules contain at least two double bonds? 1 unsaturated fatty acid 2 collagen 3 haemoglobin A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: A
10 The diagram shows a protein molecule. globular head key long polypeptide short polypeptide Two long polypeptides each form α-helices for much of their length and these twist together into a fibre. At one end, each of these polypeptides coils into a globular head. Two short polypeptides bind to each globular head. What describes the protein structure of this molecule? A quaternary structure because each molecule consists of six polypeptides B secondary structure because the long polypeptides form α-helices C tertiary structure because the α-helices form a fibre D tertiary structure because the heads form globular proteins
1 marks
Answer: A
11 Which types of bond will keep a folded protein in its precise shape for the longest time as the temperature rises? A disulfide B hydrogen C hydrophobic interactions D ionic
1 marks
Answer: A
11 What occurs during the formation of a peptide bond between two amino acids? A OH is removed from COOH and H is removed from an R group. B OH is removed from COOH and H is removed from NH2. C H is removed from COOH and OH is removed from an R group. D O is removed from COOH and 2H is removed from NH2.
1 marks
Answer: B
8 The diagram shows a small part of a polypeptide. CH3 CH3 H O CH H CH N C CH N C CH N C H H O CH CH3 O CH2 CH3 What would the products be if the part shown was completely hydrolysed? H O H O H O A H N C C H N C C H N C C H OH OH CH OH CH CH3 CH3 CH3 CH2 CH3 H H O H H O H H O B N C C N C C N C C H H H H H H CH H CH CH3 CH3 CH3 CH2 CH3 H O H O H O C N C C N C C N C C H H OH H OH H CH OH CH CH3 CH3 CH3 CH2 CH3 H H O H H O H H O D N C C N C C N C C H H OH H OH H CH OH CH CH3 CH3 CH3 CH2 CH3
1 marks
Answer: D
9 The enzyme trypsin hydrolyses proteins to amino acids. Trypsin does not function when the pH is very low as its 3D shape would be changed. What explains this change in 3D shape? A Hydrogen ions attach themselves to negatively charged R groups. B Hydrogen ions disrupt disulfide bonds. C Hydrogen ions increase hydrogen bonding between amino acids. D Hydrogen ions reduce the affinity of hydrophilic R groups for water.
1 marks
Answer: A
10 The flow chart shows some of the steps in the formation of collagen. three polypeptide chains held together by X bonds triple helix held together by intermolecular bonds Y Z Which row correctly identifies X, Y and Z? X Y Z A disulfide fibres fibrils B hydrogen fibrils fibres C hydrogen microfibrils fibres D peptide and hydrogen fibres microfibrils
1 marks
Answer: B
11 Which molecules contain at least two double bonds? 1 saturated fatty acid 2 collagen 3 haemoglobin A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: D
9 Which molecules are formed by condensation which involves a carboxyl group? A amylopectin, collagen, triglyceride, sucrose B amylopectin, collagen, triglyceride C amylopectin, -globin, sucrose D collagen, -globin, triglyceride
1 marks
Answer: D
10 Which row correctly matches the function with the structural features of cellulose, collagen, glycogen or triglyceride? structure molecules held molecule function fibrous together by branched chains hydrogen bonds A cellulose support Jv Jv x triglyceride | energy source x x x B collagen strengthening Jv Jv x cellulose support Jv x v Cc collagen strengthening Jv Jv Jv glycogen storage x x Jv D glycogen storage x Jv Jv x Jv x triglyceride energy source key J/=correct X = not correct
1 marks
Answer: A
11 The diagram shows the amino acids in a polypeptide. key type of amino acid polar basic polar acidic Asp Arg Lys polar Cys Thr Lys Leu non-polar Pro Asn Arg Val Ser Asn Glu Lys Thr Arg Phe Met Lys Phe Gln Met Ala His Val Gln Met Ala His Asn Asp Ala Glu Cys Thr Ser C terminal end Tyr Ser Glu Asn Lys Ser Thr Ser Ser N terminal end Ser Ala Ala An enzyme catalyses the hydrolysis of any peptide bond between a non-polar amino acid and any polar amino acid. How many small peptides and single amino acids will be formed by the action of this enzyme? small single peptides amino acids A 6 1 B 8 1 C 12 3 D 13 4
1 marks
Answer: D
7 A student carried out tests for biological molecules on the same sample of milk. The tests and their results were as follows. ● Heating to 80 C with Benedict’s solution gave a red colour. ● Boiling with acid, followed by neutralisation, then heating to 80 C with Benedict’s solution also gave a red colour. ● Adding Biuret solution gave a purple colour. ● Adding iodine solution gave a yellow colour. Which biological molecules must be present in the milk? 1 non-reducing sugars 2 protein 3 reducing sugars 4 starch A 1, 2 and 3 B 1 and 2 only C 2 and 3 only D 3 and 4
1 marks
Answer: C
12 Adult human haemoglobin typically consists of two chains and two chains. Approximately 5% of humans have one amino acid in the chain that has been changed. This change affects the structure and stability of haemoglobin. Which levels of protein structure could be affected in the haemoglobin of the humans with the changed amino acid? A primary only B primary and quaternary only C secondary, tertiary and quaternary only D primary, secondary, tertiary and quaternary
1 marks
Answer: D
13 Lysozyme occurs in human tears, saliva, milk and mucus. Lysozyme has a role in the immune system and hydrolyses peptidoglycan. Which description of lysozyme is correct? A It is an extracellular antibody. B It is an intracellular antibody. C It is an extracellular antibacterial protein. D It is an intracellular antibacterial protein.
1 marks
Answer: C
12 Which statement about collagen is correct? A Tissues containing collagen fibres cannot stretch. B Each polypeptide chain forms an alpha helix. C Three helices are held together by hydrogen bonds. D Three polypeptide chains form a single collagen fibre.
1 marks
Answer: C
8 Which pair of molecules only includes macromolecules that can be found in animal cells? A amylase and amylopectin B collagen and glycogen C deoxyribose and starch D sucrose and haemoglobin
1 marks
Answer: B
11 Which description of collagen is correct? A A collagen molecule consists of three polypeptide chains, each in the shape of a helix. The three chains are wound together into a triple helix called a fibre. B A collagen molecule consists of three polypeptide chains, each of which is an -helix. The three chains are wound tightly together into a triple helix. Many of these triple helices bind together as a fibre. C A collagen molecule consists of three polypeptide chains wound tightly into a triple helix called a fibre. D A collagen molecule consists of three polypeptide chains in which every third amino acid is glycine. The three polypeptides are wound tightly together into a triple helix. Many of these helices form a fibre.
1 marks
Answer: D
12 In a healthy human, the mean value for the number of haemoglobin molecules in one red blood cell is 260 million. How many -globin chains does one red blood cell contain in a healthy human? A 1.3 108 B 2.6 108 C 5.2 108 D 1.04 109
1 marks
Answer: C
13 Which statements about a peptide bond are correct? 1 It joins two monomers which are always identical to each other. 2 It contains four different atoms. 3 It can be broken by the addition of water at room temperature. 4 It is important in the primary structure of proteins. A 1, 2 and 3 B 1 and 3 only C 2, 3 and 4 D 2 and 4 only
1 marks
Answer: D
11 Which molecule contains the smallest number of hydrogen atoms? A -glucose B glycine, an amino acid in which the R group is H C glycerol D a saturated fatty acid containing eight carbon atoms
1 marks
Answer: B
11 Which molecules contain at least three double bonds? A saturated fatty acid, collagen and haemoglobin B collagen and saturated fatty acid C haemoglobin and collagen D saturated fatty acid and haemoglobin
1 marks
Answer: C
12 The diagrams show the structures of two amino acids. One contains two amino (–NH2) groups, labelled 1 and 2. The other contains two carboxylic (–COOH) groups, labelled 3 and 4. 2 3 H2N CH COOH H2N CH COOH CH2 CH2 C 1 COOH 4 O NH2 A peptide bond is formed between the two amino acids. Which groups form the peptide bond? A 1 and 4 B 2 and 3 C 2 and 4 D 1 and 3
1 marks
Answer: B
13 Which row about the structure of proteins is correct? primary structure secondary structure tertiary structure quaternary structure A is the number is the right-handed is the result of is the sub-unit of amino acids spiral formed by the cross-bonding polypeptides that present in a protein primary structure between specific link together to amino acids in form a protein the primary structure B is the order of is the coiling of a is the shape formed contains two types amino acids present chain of amino acids by the folding of a of polypeptide that in a protein to form a -pleated polypeptide and is interact forming the encoded by DNA sheet or an -helix held together by shape of a protein hydrogen bonds C is the result of occurs because of an is the result of ionic is formed by four translation of an attraction between and hydrogen bonds, polypeptides and mRNA molecule by hydrogen and disulfide bridges an additional a ribosome into a oxygen atoms in and hydrophobic reactive group chain of amino acids the peptide bonds interactions between attached to the amino acids protein D is the sequence is formed by is formed as a result is formed by the of amino acids in hydrogen bonding of interaction of the linking together a protein coded by between amino acids side chains of of more than one an mRNA molecule forming the amino acids in the polypeptide to primary structure primary structure form a protein
1 marks
Answer: D
10 The diagrams show three examples of different bonds. bond 2 bond 1 bond 3 O NH O C C N CH2 S S CH2 H Which bonds hold the tertiary structure of proteins together? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: C
11 Which feature of collagen enables it to fulfil a structural role in skin and in tendons? A Adjacent collagen molecules are linked by ester bonds. B Collagen fibres form layers with the fibres in different directions. C Collagen molecules are formed as a triple helix of polypeptide chains. D Polypeptide chains of collagen are tightly folded into compact shapes.
1 marks
Answer: C
11 Which molecules contain at least two double bonds? A saturated fatty acid, collagen and haemoglobin B collagen and saturated fatty acid only C haemoglobin and collagen only D saturated fatty acid and haemoglobin only
1 marks
Answer: C
12 The diagram shows an amino acid. H CH3 O N C C H H OH Which group is changed to produce different amino acids? A OH B C=O C CH3 D NH2
1 marks
Answer: C
13 Which row is correct about the structure of proteins? primary secondary tertiary quaternary A determined by occurs by disulfide, ionic, always formed by the sequence of hydrogen bonding hydrogen bonds association of two DNA nucleotides between NH and and hydrophobic or more C=O groups of interactions are all polypeptides amino acids involved B the number of in a single the bonds are always formed by amino acids in polypeptide it is formed at specific two or more each polypeptide either an -helix points determined polypeptides held chain or a -pleated by the primary together by bonds sheet structure formed between the polypeptides C formed by an -helix is only globular always formed twenty different formed by proteins have this by two or amino acids hydrogen bonds level of structure more different linked in a between side polypeptides to specific order chains of give the final shape amino acids D the sequence a -pleated sheet reactions between always formed of amino acids in is the result of a side chains of by two or each polypeptide folded specific amino more polypeptides chain polypeptide acids give a and a metal ion forming hydrogen specific 3-D shape bonds between adjacent strands
1 marks
Answer: A
7 Which tests will identify biological molecules that contain monomers with a carboxyl group? Benedict’s D A biuret ethanol C B
1 marks
10 Which molecules always contain at least four double bonds? A triglyceride, collagen and haemoglobin B collagen and triglyceride only C haemoglobin and collagen only D triglyceride and haemoglobin only
1 marks
Answer: C
11 Which row about the structure of proteins is correct? primary structure secondary structure tertiary structure A the number the left-handed the result of of amino acids spiral formed by the cross-bonding between present in a protein primary structure specific amino acids in the primary structure B the order of the coiling of a the shape formed amino acids present chain of amino acids by folding of a in a protein to form a -pleated polypeptide and encoded by DNA sheet held together by hydrogen bonds C the result of occurs because of the result of ionic translation of an attraction between and hydrogen bonds, mRNA molecule by hydrogen and disulfide bridges a ribosome into a oxygen atoms in and hydrophobic chain of amino acids the side chains interactions between amino acids D the sequence formed by formed as a result of amino acids in hydrogen bonding of interaction of the a protein coded by between amino acids side chains of an mRNA molecule forming the amino acids in the primary structure primary structure
1 marks
Answer: D
12 Which statement about collagen is correct? A A collagen fibre is made of three parallel helices with hydrogen bonds holding them in place. B It is an insoluble fibrous protein with a quaternary structure. C One-third of the amino acids making up collagen are valine. D Collagen fibres are formed from several collagen molecules held together by ionic bonds.
1 marks
Answer: B
14 Which descriptions about all enzymes are correct? 1 catalyse the breakdown of large molecules into smaller molecules 2 only function inside cells 3 form temporary bonds with the substrate 4 have a tertiary structure A 1 and 2 B 1 and 3 C 2 and 3 D 3 and 4
1 marks
Answer: D
9 Which row matches each molecule to a type of bond that is present? ester bond hydrogen bond disulfide bond A amylase haemoglobin catalase B glycerol glycogen collagen C lipid amylopectin amylose D phospholipid cellulose antibody
1 marks
Answer: D
14 The diagrams show three examples of different bonds. bond 2 bond 1 bond 3 O NH O C N CH2 S S CH2 H Which bonds can hold the quaternary structure of proteins together? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: C
15 Which row correctly describes the primary structure, secondary structure, tertiary structure and quaternary structure of some proteins? primary secondary tertiary quaternary structure structure structure structure A determines the depends on defines the overall formed when two folding of the hydrogen bonding shape and folding or more identical polypeptide between the of the protein polypeptides join side-chains of together amino acids B defines the order usually forms is held together by found in globular of amino acids in immediately after all the types of proteins such as the polypeptide polypeptide bonding that haemoglobin but synthesis occur in proteins never in fibrous proteins C involves covalent involves essential for the formed when two bonds only interactions function of or more between –H and enzymes and polypeptides join =O receptors together D involves peptide involves folding changes can involve bonds between between local reversibly when hydrogen bonds, the side-chains of regions within a bound to covalent bonds amino acids polypeptide non-competitive and hydrophobic molecule inhibitors interactions
1 marks
Answer: C
10 A polypeptide contains a specific number of amino acids, n. How many peptide bonds are present in this polypeptide? A n – 1 B n C n + 1 D n + 2
1 marks
Answer: A
11 Which statement is correct? A Amylase, ribose and phospholipid are all macromolecules. B Cellulose, glucose and catalase are all polymers. C Deoxyribose, fructose and ribose are all monosaccharides. D Sucrose, deoxyribose and amylopectin are all polysaccharides.
1 marks
Answer: C
12 A student used colorimetry to monitor the hydrolysis of a protein by a protease enzyme. The student used biuret solution to determine the concentration of protein in the hydrolysis reaction. The student produced a calibration curve using known concentrations of protein. Which diagram shows the calibration curve? A B transmission absorbance 0 0 0 protein 0 protein concentration concentration C D transmission absorbance 0 0 0 protein 0 protein concentration concentration
1 marks
Answer: B
8 Which statement is correct? A Cellulose, glycogen and amylopectin are all polymers. B Ribose, amylase and phospholipid are all macromolecules. C Starch, glucose and amylose are all monomers. D Sucrose, deoxyribose and amylopectin are all polysaccharides.
1 marks
Answer: A
9 The diagram shows two amino acids. Some of the hydrogen atoms are numbered 1 to 6. H H O H H O N C C N C C H H OH H H OH 1 2 3 4 5 6 Which two numbered hydrogen atoms could contribute to the production of a molecule of water when a peptide bond forms between these two amino acids? A 1 and 4 B 1 and 6 C 3 and 5 D 2 and 4
1 marks
Answer: B
11 Typical enzymes are large globular proteins with a specific tertiary shape. Which molecular interactions are directly involved in maintaining the tertiary shape? 1 hydrogen bonding 2 disulfide bridges 3 hydrophobic interactions A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: A
11 Which molecule contains at least one peptide bond? A B H H O OH HO CH2 C C H C O C R O H O O N HO C CH2 C C H H C O C R H O O N CH3 C C H H C O C R O N H H H C D HOCH2 NH2 CH2OH OH OH C N H O H C N H H H H HC H2 C CH OH H C N N HO O O CH2OH O O H OH –O HC CH P CH CH O O OH
1 marks
Answer: B
12 RNA polymerase and peptidyl transferase are both enzymes involved in protein synthesis. Which statements describe similarities between these two enzymes? 1 They are both globular proteins. 2 They both have the same tertiary structure. 3 They are both intracellular enzymes. A 1 and 2 B 1 and 3 C 1 only D 2 and 3
1 marks
Answer: B
17 The diagram shows a section of a glycoprotein molecule found embedded in a cell surface membrane. Each of the amino acids is represented by a small shaded circle. amino acid Q amino acid chain forms an alpha helix Which row shows a property of the amino acids found in the alpha helix and a property of amino acid Q? property of property of amino acids found amino acid Q in the alpha helix A non-polar polar B non-polar non-polar C polar polar D polar non-polar
1 marks
Answer: A
8 Which row correctly matches the example with the type of molecule? disaccharide macromolecule monomer polymer A fructose glycogen glucose starch B starch haemoglobin ribose glycogen C maltose ribonucleic acid sucrose cellulose D sucrose cellulose fructose collagen
1 marks
Answer: D
11 Bread contains a mixture of polypeptides known as gluten. Two of the polypeptides found in gluten are glutenin and gliadin. Which statement describes the tertiary structure of a protein? A Disulfide bonds form between glutenin and gliadin. B A large proportion of the amino acids in gliadin are glutamine. C α-helical sections are found in glutenin and gliadin. D Amino acids with hydrophobic R groups are found on the inside of glutenin.
1 marks
Answer: D
34 A shortage of protein in the diet of children can lead to a disease that causes excess tissue fluid to build up in the abdomen. What explains why a build-up of excess tissue fluid can occur in this disease? A A shortage of plasma proteins decreases blood water potential; less tissue fluid returns to the blood. B A shortage of plasma proteins increases blood water potential; less tissue fluid returns to the blood. C A shortage of protein in the diet causes weak cardiac muscle, reducing hydrostatic pressure. D A shortage of protein in the tissue fluid decreases its water potential; more water leaves the blood.
1 marks
Answer: B
11 Silk moth caterpillars have been genetically modified to produce a mixture of their own silk and the much stronger spider silk of the golden orb web spider. The spider silk polypeptide chain has many repeated sequences of two amino acids, glycine and alanine, arranged in a crystalline structure. What correctly describes the structure of spider silk? A primary protein structure with regions of α-helices B secondary protein structure with regions of β-pleated sheets C tertiary protein structure with regions of α-helices D quaternary protein structure with regions of β-pleated sheets
1 marks
Answer: B
12 Which property of the tertiary structure of a globular protein enables it to catalyse a metabolic reaction? A It has hydrophobic amino acid R groups on the outside. B It will be denatured by high temperatures. C The R groups of some amino acids form bonds with a substrate. D The three-dimensional shape depends on hydrogen bonding.
1 marks
Answer: C
40 A student wrote three statements about antibodies. 1 Their structure depends on peptide, hydrogen and disulfide bonds. 2 They are protein molecules with both tertiary and quaternary structure. 3 Four polypeptides provide four antigen binding sites. Which statements are correct? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: B
11 A scientist studying the structure of a protein reported that it consists of two polypeptide chains joined by disulfide bonds. Which feature of protein structure does this describe? A primary structure B secondary structure C tertiary structure D quaternary structure
1 marks
Answer: D
11 Which row correctly shows levels of protein structure that can be held together by each type of interaction? hydrophobic hydrogen bonds covalent bonds interactions A primary, secondary tertiary structure primary and and tertiary structure tertiary structure B secondary structure primary and tertiary structure tertiary structure C secondary and tertiary structure primary and tertiary structure tertiary structure D secondary and tertiary structure primary and tertiary structure secondary structure
1 marks
Answer: C
12 Which molecules contain at least three double bonds? saturated triglyceride C A D collagen B haemoglobin
1 marks
Answer: D
9 The diagrams show three examples of different bonds. bond 1 bond 2 bond 3 O NH O C C N CH2 S S CH2 H Which bonds hold the secondary structure of proteins together? A 1, 2 and 3 B 1 and 3 only C 1 only D 2 and 3 only
1 marks
Answer: C
10 Insulin is a globular protein involved in cell signalling. It is transported in the blood plasma from the cells that synthesise it to its target cells. A molecule of insulin contains six sulfur-containing amino acids and has two polypeptide chains. Which statements about insulin are correct? 1 An insulin molecule has a quaternary structure. 2 Insulin polypeptides are held together by six disulfide bonds. 3 Amino acids with hydrophobic R groups would be found in the centre of an insulin molecule. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: C
9 Which molecules contain at least two double bonds? sucrose C A D collagen haemoglobin B
1 marks
Answer: B
11 Which part of the structure of haemoglobin carries oxygen? A four polypeptide chains B haem groups C hydrogen bonds D hydrophilic R groups
1 marks
Answer: B
5 Which polymers are present in all viruses, all prokaryotes and all eukaryotes? 1 polynucleotides 2 polypeptides 3 polysaccharides A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: B
11 Which molecules contain at least four double bonds? unsaturated triglyceride C A D haemoglobin collagen B
1 marks
Answer: D
12 The diagram shows the amino acid glutamic acid. COOH H C CH2 CH2 COOH NH2 What is the R group for glutamic acid? A NH2 B H C COOH D CH2 CH2 COOH
1 marks
Answer: D
13 The diagram shows three interactions that hold protein molecules in shape. N H NH3 + O S S interaction 1 interaction 3 C COO– S S interaction 2 Which row identifies these interactions? interaction 1 interaction 2 interaction 3 A hydrogen bond disulfide bond hydrophobic interaction B hydrogen bond covalent bond ionic bond C hydrophobic interaction ionic bond hydrogen bond D ionic bond disulfide bond peptide bond
1 marks
Answer: B
14 Some animals produce antimicrobial proteins which protect them from pathogens. These proteins could be used to kill human pathogens, however when used as a medicine they are broken down by protein-digesting enzymes. Replacing one of the amino acids found in the protein with an amino acid that had been synthesised in the laboratory resulted in a modified protein that was not broken down. What could explain why this modified protein was not broken down by the protein-digesting enzymes? 1 The modified protein has a different tertiary structure to the original protein. 2 The modified protein is not complementary in shape to the enzyme’s active site. 3 The modified protein is unable to induce a fit with the protein-digesting enzyme. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: A
7 Which bonds are present in all viruses? 1 phosphodiester 2 peptide 3 covalent A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: A
11 The diagram represents an amino acid. H R O N C C H H OH R represents a variable side chain. What is not a possible side chain? A CH3 B CH2CH2SCH3 C CH2CONH2 D HOCH2CH(OH)CH2OH
1 marks
Answer: D
9 Which molecules have a structural formula that contains C=O bonds? 1 amino acids 2 fatty acids 3 glycerol 4 protein A 1, 2 and 3 B 1, 2 and 4 C 1, 3 and 4 D 2, 3 and 4
1 marks
Answer: B
12 The diagram shows the structure of part of a peptidoglycan molecule. H CH2OH H O O H OH H H O H H O O O H CH2OH H3C CH C O NH HC CH3 CO NH HC (CH3)2COOH CO NH NH2 HC (CH3)2CHCOOH CO NH HC COOH CH3 Which type of 1,4 linkage and how many peptide bonds are shown in this part of the molecule? type of number of 1,4 linkage peptide bonds A α-1,4 3 B α-1,4 4 C β-1,4 3 D β-1,4 4
1 marks
Answer: D
6 The diagrams show the structure of four amino acids in aqueous solution. COO– COO– H C H3N+ CH2 CH2 CH2 CH2 C N+H3 N+H3 H H glycine lysine COO– O COO– CH3 C C CH2 C N+H3 O– N+H3 H H alanine aspartate Which two structures have an overall charge? A alanine and aspartate B alanine and glycine C aspartate and lysine D glycine and lysine
1 marks
Answer: C
8 Collagen molecules are made up of three polypeptide chains interacting together. The individual polypeptide chains consist of a regular pattern of amino acids. Almost every third amino acid is glycine. Which protein structures of collagen are described? A primary and secondary B primary and quaternary C secondary and tertiary D tertiary and quaternary
1 marks
Answer: B
9 The masses of the parts of haemoglobin are shown in the table. component mass / Da -globin chain 15 126 -globin chain 15 868 haem group 15 617 There are 1000 Da in 1 kDa. What is the mass of a haemoglobin molecule in kDa? A 31.6 B 33.5 C 62.6 D 64.5
1 marks
Answer: D
14 The diagram shows a simple metabolic pathway. W X Y Z The letters W, X, Y and Z represent four different substances. At each step in the diagram the substrate undergoes a chemical reaction catalysed by an enzyme. The reaction produces the next substance in the pathway. Which statements correctly describe the enzymes taking part in this metabolic pathway? 1 They are all globular proteins. 2 They all have the same tertiary structure. 3 They all contain hydrogen atoms in their structure. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 only
1 marks
Answer: C
7 Which statements about peptide bond formation are correct? 1 The bond formation occurs between a carbon of one amino acid and a nitrogen of the next amino acid after the amino acids detach from tRNA. 2 The bond formation occurs at the ribosome while the amino acids are still attached to tRNA, and is a hydrolysis reaction. 3 The bond formation is important for growth of an organism and when the bond forms, a water molecule is removed. A 1 and 3 B 2 and 3 C 2 only D 3 only
1 marks
Answer: D
12 Which row correctly identifies the weak and strong bonds in the tertiary and quaternary structure of a typical protein? type of bond disulfide hydrogen hydrophobic ionic A strong strong weak weak B strong weak weak weak C weak weak strong strong D weak weak weak strong
1 marks
Answer: B
13 Which row correctly describes haemoglobin? A four polypeptide iron ions can in each chain, at 50% saturation, chains, each associate with hydrophobic R-groups two oxygen containing a oxygen, forming of amino acids point molecules are haem group oxyhaemoglobin towards the centre of transported by the the molecule molecule B polypeptide chains each chain consists of two each chain can interact to produce a contains a haem identical alpha chains transport an globular chain group of amino and two identical oxygen molecule acids surrounding beta chains an iron ion C polypeptide chains an iron ion is quaternary structure each molecule can interact to produce present within each has two alpha chains transport a total of an almost spherical haem group and two beta chains four oxygen atoms molecule D polypeptide chains iron ions in the in each chain, each molecule can produce a loose molecule can bind hydrophobic R-groups transport a total of helical shape, which reversibly with of amino acids eight oxygen atoms folds to form a oxygen surround the iron ion spherical molecule
1 marks
Answer: A
8 What cannot occur as a result of a condensation reaction? A breaking of a glycosidic bond B formation of a disaccharide C joining together of two amino acids D production of a molecule of water
1 marks
Answer: A
9 Which fact about the quaternary structure of proteins is correct? A consists of four polypeptides B depends on the presence of metal ions C depends on the primary structure of the polypeptides D is made of and polypeptides
1 marks
Answer: C
11 The diagrams show parts of three pairs of amino acids within a protein. The pairs are labelled X, Y and Z. X Y Z H H CH3 H3C O O C O O C C C C C H H H H H CH3 H3C H NH3 + –O Which row shows the correct type of interaction that would occur between the two amino acids in each pair? X Y Z A hydrophobic interaction hydrophobic interaction hydrogen bond B hydrogen bond hydrophobic interaction ionic bond C hydrogen bond hydrogen bond hydrogen bond D hydrophobic interaction hydrogen bond ionic bond
1 marks
Answer: B
6 The diagram shows part of a collagen fibril made of collagen triple helices. The collagen triple helices are linked to each other by one type of bond. This bond is labelled as X in the diagram. X collagen fibril collagen triple helix What is bond X? A covalent bond B disulfide bond C hydrogen bond D peptide bond
1 marks
Answer: A
7 The table shows some information about the polypeptides that make up haemoglobin. -globin -globin total number of amino acid 141 146 residues in polypeptide chain position of amino acid cysteine 104 93 and 112 in polypeptide chain Scientists studied the region of the -globin polypeptide chain containing the amino acid cysteine at position 93. They found that: ● this region faces outwards when no oxygen is attached to the haem group ● this region faces inwards when oxygen is attached to the haem group ● replacing cysteine with a different amino acid reduces the Bohr shift. What can be concluded from the information about cysteine in haemoglobin? A More than 1% of the amino acids in one haemoglobin protein are cysteine. B In -globin, there is a cysteine closer to the end of the polypeptide chain with an unreacted carboxyl group than in -globin. C The replacement of the cysteine at position 93 in -globin decreases the affinity of haemoglobin for oxygen at low pH. D The binding of oxygen to the haem group causes the region of -globin containing cysteine at position 93 to become more hydrophilic.
1 marks
Answer: A
11 Which molecules are globular proteins? 1 amylase 2 haemoglobin 3 DNA polymerase A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 only
1 marks
Answer: A
7 Which description lists all the components of a human haemoglobin molecule? A four polypeptides that are all the same and one haem group B four polypeptides that are not all the same and one haem group C four polypeptides that are all the same and four haem groups D four polypeptides that are not all the same and four haem groups
1 marks
Answer: D
8 HIV-1 protease is an enzyme produced by the HIV virus. Two identical chains of 99 amino acids form the enzyme. In each chain, amino acids 25, 26 and 27 in the sequence form part of the active site. Which orders of protein structure control the shape of the active site? A primary, secondary, tertiary and quaternary B primary, secondary and tertiary only C primary and quaternary only D quaternary only
1 marks
Answer: A
12 Which statements could be used to describe enzyme molecules and antibody molecules? 1 Hydrogen bonds stabilise the structure of the protein and are important for it to function efficiently. 2 Hydrophilic R-groups point in to the centre of the molecule and cause it to curl into a spherical shape. 3 The tertiary structure of the protein molecule plays an important role in the functioning of the protein. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: C
10 Hydroxyproline is synthesised by addition of an –OH group to the R-group of the amino acid proline. Hydroxyproline is a major component of collagen and has an important role in increasing the stability of its structure. Which statement explains why the addition of an –OH group to proline could increase the stability of collagen? A It strengthens hydrogen bonding between the R-groups of adjacent polypeptide chains, resulting in a tertiary structure that is more resistant to heat denaturation. B It increases the number of sites available for the formation of hydrogen bonds within the secondary structure of collagen, resulting in more stable alpha helices. C It increases the formation of hydrogen bonds between R-groups and water molecules, which help to hold the chains of the collagen triple helix together by strengthening hydrophilic interactions. D It strengthens the quaternary structure of collagen by providing more sites for hydrogen bonding between the R-groups of distantly separated amino acids within the same polypeptide chain.
1 marks
Answer: C
13 Which levels of protein structure are always involved in forming the active site of an enzyme? level of protein structure primary tertiary quaternary key v= always involved X = not always involved
1 marks
Answer: B
38 The diagrams show three different bonds. 1 2 3 O H H N H O C N C S S C H H H Which bonds are found in an antibody molecule? A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 2 and 3 only
1 marks
Answer: A
8 Which molecules contain at least two double bonds? saturated triglyceride C A D collagen haemoglobin B
1 marks
Answer: D
11 Which bonds are found in the levels of structure of a protein molecule? primary structure secondary structure quaternary structure A covalent bond hydrogen bond peptide bond B covalent bond ionic bond disulfide bond C peptide bond hydrogen bond ionic bond D peptide bond ionic bond disulfide bond
1 marks
Answer: C
11 Which molecules have products containing a carboxyl group when they are hydrolysed? 1 phospholipids 2 polysaccharides 3 proteins A 1 and 2 B 1 and 3 C 2 and 3 D 3 only
1 marks
Answer: B
12 Which bonds are involved in maintaining the secondary and tertiary levels of protein structure? 1 disulfide 2 hydrogen 3 ionic secondary tertiary A 2 only 1, 2 and 3 B 2 and 3 only 2 and 3 only C 1 and 3 only 1 and 3 only D 1, 2 and 3 1 only
1 marks
Answer: A
13 The diagrams show the structure of four amino acids in solution. glycine lysine COO– COO– H C H3N+ CH2 CH2 CH2 CH2 C NH3 + NH3 + H H alanine aspartate COO– O COO– H3C C C CH2 C NH3 + O– NH3 + H H Which amino acids have no overall charge? A alanine and aspartate B alanine and glycine C aspartate and lysine D glycine and lysine
1 marks
Answer: B
15 Histidine and proline are two amino acids commonly found in enzymes. Histidine has a polar R-group and proline has a non-polar R-group. Where would most histidines and prolines be positioned? histidine proline A inside an enzyme on the surface of an enzyme B on the surface of an enzyme on the surface of an enzyme C inside an enzyme inside an enzyme D on the surface of an enzyme inside an enzyme
1 marks
Answer: D
10 Which molecules contain at least two double bonds? unsaturated fatty acid C A D collagen haemoglobin B
1 marks
Answer: D
11 Which description of globular proteins is correct? A They are only found in cell surface membranes. B They only contain amino acids with hydrophilic R groups. C They can change shape by using energy from ATP. D They always have a quaternary structure of at least three polypeptides.
1 marks
Answer: C
8 Which diagram has a covalent bond that joins monomers together to form a biological polymer in eukaryotes? A B C D O R H O R O R R NH3 + –O C R C O R O R O P O R O–
1 marks
Answer: D
10 Which molecules contain at least four double bonds? saturated triglyceride C A D collagen haemoglobin B
1 marks
Answer: B
11 In some people a mutation can affect the beta chains in their haemoglobin molecules. As a result polar amino acids on the outer surfaces of the chains are replaced by non-polar amino acids. What will be the effect on haemoglobin? A Haemoglobin will become less soluble. B Haemoglobin will become more soluble. C Hydrophobic interactions between amino acids will decrease. D More hydrogen bonds will form in the molecule.
1 marks
Answer: A
9 Many biological molecules exist as polymers made up of monomer subunits. Which row correctly identifies the monomer in each of the biological molecules? collagen glycogen cellulose A amino acid -glucose -glucose B -glucose -glucose amino acid C -glucose amino acid -glucose D amino acid -glucose -glucose
1 marks
Answer: A
15 Which descriptions of enzymes that use the lock-and-key hypothesis are correct? 1 The active site is complementary to the substrate the enzyme acts on. 2 Bonds that form in the enzyme–substrate complex change the shape of the active site. 3 Most of the amino acids in an enzyme help to maintain the specific shape of the enzyme. A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 3 only
1 marks
Answer: C