Question 1
25 marksWrite an essay on the following topic.
The importance of changes in the shape of protein molecules in organisms.
Model answer
The function of a protein depends on its tertiary structure, the three-dimensional shape held by hydrogen bonds, ionic bonds and disulfide bridges between R-groups. Many proteins work because this shape changes when another molecule binds, and these changes are important throughout organisms.
Enzymes work by the induced-fit model. The active site is not exactly complementary to the substrate, but when the substrate binds the active site changes shape slightly to mould around it, forming an enzyme-substrate complex. This puts strain on bonds in the substrate, or brings reacting groups close together, so the activation energy is lowered. Changes in enzyme shape also control metabolism. A non-competitive inhibitor binds to a site other than the active site and changes the shape of the active site, so substrates can no longer bind; this allows the end product of a pathway to switch off an earlier enzyme. Harmful changes in shape also matter: high temperature breaks hydrogen bonds and extremes of pH disrupt ionic bonds, so the enzyme is denatured. This is why mammals keep a stable core temperature and blood pH.
Haemoglobin is a protein with a quaternary structure of four polypeptides, each with a haem group that binds one oxygen molecule. When the first oxygen binds, the shape of haemoglobin changes so that it becomes easier for further oxygen molecules to bind (cooperative binding). This produces the S-shaped oxyhaemoglobin dissociation curve, so saturation changes a lot over a small range of partial pressures of oxygen; haemoglobin loads oxygen readily in the lungs and unloads it readily in respiring tissues. Carbon dioxide also changes the shape of haemoglobin: it lowers the pH, which reduces haemoglobin's affinity for oxygen (the Bohr effect), so more oxygen is unloaded where cells are respiring fastest. Different haemoglobins differ in how readily they bind oxygen: animals that live where oxygen is scarce have haemoglobin with a higher affinity, so their dissociation curve lies to the left and their haemoglobin still becomes saturated.
Carrier proteins in cell membranes change shape to move substances. In active transport, a molecule or ion binds to a specific carrier, ATP is hydrolysed and a phosphate attaches to the carrier, which changes shape and releases the substance on the other side of the membrane. The sodium-potassium pump moves three sodium ions out of a cell for every two potassium ions moved in. This is important because it maintains the sodium ion gradient used in co-transport, for example when glucose is absorbed by epithelial cells in the ileum against its concentration gradient, and it helps to maintain the resting potential of neurones.
Channel proteins that open by changing shape allow cells to respond to stimuli. In a Pacinian corpuscle, pressure deforms the lamellae and stretches the membrane of the sensory neurone, so stretch-mediated sodium ion channels open; sodium ions diffuse in and produce a generator potential. At a cholinergic synapse, acetylcholine binds to receptor proteins on the postsynaptic membrane, which change shape and open sodium ion channels, depolarising the membrane. Acetylcholinesterase then hydrolyses the acetylcholine, so the channels close again. This is important because it means a response occurs only when a stimulus or neurotransmitter is present, and it stops continuous stimulation of the postsynaptic neurone. Some drugs act on these receptors: a drug that binds to the acetylcholine receptor but does not cause the change in shape that opens the channel blocks transmission, which is how some muscle relaxants used in surgery work.
Muscle contraction depends on changes in protein shape. When an action potential reaches a muscle fibre, calcium ions are released from the sarcoplasmic reticulum and cause tropomyosin to move, exposing the binding sites on actin. Myosin heads bind to actin, forming actinomyosin cross-bridges. Each myosin head then changes angle, pulling the actin filament towards the centre of the sarcomere as ADP and phosphate are released. ATP binds and the head detaches, and hydrolysis of ATP returns the head to its original position, ready to bind again. These repeated changes in shape shorten sarcomeres, so muscles can contract and move parts of the skeleton.
Changes in the shape of proteins also control gene expression. The steroid hormone oestrogen is lipid-soluble, so it diffuses through the cell-surface membrane and binds to a site on a transcription factor in the cytoplasm. This changes the shape of the transcription factor, releasing it from an inhibitor molecule. It can then enter the nucleus and bind to the promoter of a target gene, stimulating RNA polymerase to transcribe it. This is important because only cells with the right receptor respond, so one hormone can control specific genes in specific tissues.
Changes in protein shape can also be harmful. Prions are abnormally folded forms of a normal brain protein. When a prion contacts the normal protein, it causes it to fold into the abnormal shape, so the abnormal form accumulates, forms insoluble clumps and kills neurones, causing diseases such as variant CJD. This shows how completely a protein's function depends on its shape.
Explanation
Planning: choose four to six topic areas where a protein changes shape, for example induced fit and enzyme inhibition, cooperative binding of oxygen by haemoglobin, carrier proteins in active transport, gated channel proteins in receptors and synapses, myosin and tropomyosin in muscle contraction, and transcription factors. For each, describe the protein and how its shape changes (AO1) and then explain why that change matters to the cell or organism (AO2), spending about 10 minutes per topic. Every paragraph must be about a change in shape: a full account of the sliding filament theory, or of the cardiac cycle, adds nothing once the role of the protein has been explained.
Faults that lose marks: writing only about fixed complementary shapes, such as the lock-and-key model, without any change in shape; GCSE statements such as 'the enzyme stops working'; using many examples from one topic area (several enzymes count as one topic area); significant errors such as 'the active site is denatured by binding of a competitive inhibitor', 'sodium ions enter by active transport' at a synapse, or 'the actin and myosin filaments get shorter'; and describing processes outside organisms, such as PCR, which is irrelevant to a title that says 'in organisms'. For top marks include material beyond the specification at A-level depth, such as prions.
Mark scheme
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25 marks
Levels of response (25 marks).
Level 5 (21-25 marks): A holistic, fully integrated answer that makes clear links between several different topics and the theme of the question. Biology is detailed and comprehensive A-level content, uses appropriate terminology, and is very well written and always clearly explained. No significant errors or irrelevant material. For top marks in the band, the answer shows evidence of reading beyond specification requirements.
Level 4 (16-20 marks): Links several topics to the main theme of the question to form a series of interrelated points which are clearly explained. Biology is fundamentally correct A-level content with some detailed points, though some may be less well developed, and appropriate terminology. Perhaps one significant error and/or one irrelevant topic which detracts from the overall quality of the answer.
Level 3 (11-15 marks): Mostly deals with suitable topics, but they are not interrelated and links are not made to the theme of the question. Biology is usually correct A-level content, though it lacks detail; it is usually clearly explained and generally uses appropriate terminology. Some significant errors and/or more than one irrelevant topic.
Level 2 (6-10 marks): Predominantly deals with only one or two topics that relate to the question. Biology shows some superficial A-level content that may be poorly explained, lacking in detail, or show limited use of appropriate terminology. May contain a number of significant errors and/or irrelevant topics.
Level 1 (1-5 marks): Only indirectly addresses the theme of the question and merely presents a series of biological facts, usually descriptive or poorly explained and at times factually incorrect. Content and terminology are generally below A-level. May contain a large number of errors and/or irrelevant topics.
0 marks: nothing of relevance.Max 15 if the essay covers fewer than four different topic areas of the specification, each discussed in at least a few sentences. Max 10 if the essay deals with only one or two topic areas of the specification.
Definitions (AQA's commentary on the levels): a topic area is a section of the specification, such as the immune system, nerve impulses or photosynthesis; 'several' means at least four topic areas, each covered in some sentences, not just a word or two, and not many examples from one topic area; a significant error is one that significantly detracts from the biological accuracy of a described example (usually more than one word); irrelevant material is several lines (or more) that clearly fail to address the title or its theme; for top marks within a band, the answer shows evidence of reading beyond the specification, an example relevant to the title used at A-level standard. Phonetic spelling is accepted except for confusable words such as glucose, glycogen and glucagon.
Indicative content (not a checklist; any topics linked to the theme at A-level standard are credited):
- 3.1.4.1 General properties of proteins: tertiary structure held by bonds
- 3.1.4.2 Many proteins are enzymes: induced fit; inhibitors; denaturation
- 3.2.3 Transport across cell membranes: carrier proteins change shape
- 3.3.4.1 Mass transport in animals: cooperative oxygen binding; Bohr effect
- 3.6.1.2 Receptors: stretch-mediated sodium ion channels open when deformed
- 3.6.2.2 Synaptic transmission: acetylcholine opens sodium ion channels
- 3.6.3 Skeletal muscles: tropomyosin moves; myosin heads change angle
- 3.8.2.2 Regulation of transcription and translation: oestrogen changes a transcription factor
Credit other relevant topics, including material beyond the specification at A-level standard.