Question 112 marks
Question
Fig. 1.1 is a diagram of a molecule of haemoglobin. A Fig. 1.1 (a) (i) Name the structure labelled A on Fig. 1.1. …… [1] (ii) State the function of structure A. …… [1] (b) Haemoglobin is described as a globular protein. Explain why this protein is described as globular. …… [2] (c) The gene HBB codes for the β-globin polypeptide. State why a polypeptide, such as β-globin, is described as a polymer. …… [2] (d) A single base change in the DNA of the gene HBB results in a change to the amino acid sequence of β-globin. In the sequence, a single glutamic acid is replaced by valine. Outline the effects of this change in the amino acid sequence of β-globin on the structure and function of a haemoglobin molecule. …… [3] (e) Haemoglobin interacts with carbon dioxide and carbon monoxide. Outline the role of haemoglobin in the transport of carbon dioxide. …… [3] [Total: 12]
Mark scheme
1(a)(i) haem ; A heme / prosthetic group 1 I iron / iron ion / Fe / Fe2+ I porphyrin ring 1(a)(ii) one from 1 combines with / binds / carries / transports / AW, oxygen (in lungs) ; R forms bonds releases / AW, oxygen, in tissues / at low oxygen concentrations ; allows haemoglobin to transport oxygen ; 1(b) two from 2 1 spherical / ball-like / rounded / AW ; R circular / round ignore 3D shape 2 (water) soluble / forms H bonds with water ; 3 hydrophilic R-groups on outside of molecule / hydrophobic R-groups on inside ; R ref. to ‘tails’ 4 dynamic / metabolic / physiological / AW, function ; 1(c) made of amino acids ; 2 one from joined by peptide bonds ; R ‘peptide bond between two amino acids’ R ‘dipeptide bond(s)' macromolecule / long-chain (molecule) / large molecule ; repeated / many, (sub-)units / monomers ; 1(d) three from 3 1 (R-group of) glutamic acid / glu, is polar / hydrophilic and (R-group of) valine / val, is non-polar / hydrophobic ; 2 change in tertiary structure ; A ‘change in globular shape / less globular in shape’ 3 change in quaternary structure of haemoglobin ; R of β-globin 4 ref. to haemoglobin forms fibres (with other Hb) ; A ‘sticky molecules’ 5 haemoglobin is less (water) soluble ; I insoluble 6 haemoglobin is less efficient at, binding / transporting, oxygen ; A less oxyhaemoglobin A haemoglobin / β-globin, has lower affinity for oxygen A reduced oxygen carrying capacity I haemoglobin, does not / cannot, bind oxygen 7 AVP ; 1(e) three from 3 1 haemoglobin combines with carbon dioxide ; 2 carbon dioxide reacts with (terminal), amine group(s) / –NH2 / –NH ; 3 to form carbaminohaemoglobin ; R carboxyhaemoglobin / carbonylhaemoglobin 4 each polypeptide can carry a molecule of carbon dioxide / haemoglobin can carry four molecules of carbon dioxide ; 5 carbon dioxide remains, bound / AW, to Hb until in, region of low pCO2 or high pO2 / pulmonary circulation / lungs / alveoli ; 6 ref. to (carbonic acid dissociates to form) hydrogen ions, which bind to / AW, haemoglobin ; A H+ forms haemoglobinic acid or HHb I hydrogen unqualified 7 AVP ; e.g. hydrogencarbonate ions to plasma