How to Approach A level Biology Graph and Table Questions: Tips and Exam Question Pack

Get top marks when analysing figures, tables and images by avoiding common mistakes that students make

This article contains key vocabulary, a strategy for how to approach questions for success, a multichoice quiz with answers, and a big pack of past paper exam questions

Don’t panic, it’s only a graph

The single best exam tip for graphs and tables exam questions is to start by looking at the graph or chart itself. DO NOT LOOK AT THE QUESTIONS FIRST! This single thing will help you avoid the most common mistakes that students make.

But you also need to know what you’re doing. Which means you’ll need to be confident with these terms:

Background Knowledge / Vocabulary:

• Independent Variable: The variable that you purposefully set to different values during the experiment

• Dependent Variable: The variable that you measure during the experiment, which is unknown until it is measured

• Replicate: Experimental data is often replicated - the same data point is recorded multiple times for the same conditions

• Accuracy / Precision: Accuracy is how close the replicated values are to the correct value, and precision is how close they are to each other. If there is an unknown problem with the experiment, results can be very precise but have very low accuracy.

• Range / Standard Deviation: The amount of variation in the data. A large range or standard deviation means that the replicated data had a broad range of results. A small range or standard deviation means they were much more similar in value. Range / Standard deviation is therefore a measure of precision.

• Trend: What is the general relationship between the dependent and independent variables? When the experimenter increased the independent variable, what happened to the dependent variable? What shape is the graph?
  

How to Approach the Question:

1. Look at the graph or chart first!
Too many students look at the question first, get confused or panicky about what it is asking, and form preconceptions about what data they need. This then means they are then unable to look at the data clearly, and miss the information they actually need. Looking at the graph or chart first both makes the data easier to understand, and makes it easier to work out what the question is asking.

Trust me, this is a major factor in student success. If you only take away one thing from this article, always look at the graph or chart first.

2. Don’t panic if it’s about something totally unfamiliar
Students can get very thrown if the question is about an organism or molecule that they have never heard of before (the exam boards do this a lot). This sudden panic makes it hard to think clearly.

Remember - if you have covered all the course material, even if the question is about something weird and new then all the information you need will be in the data. The things that look scary are just surface details. If the question was “Fred gave James two apples, how many apples does James have” you wouldn’t need to know who these people were to answer the question.

But don’t just dive in to the details of the data …

What’s going on here?

3. Understand the format
Don’t waste time looking at the actual dots or numbers until you understand how the data has been presented. Check every aspect methodically. It’s too easy to make assumptions based on previous graph/table formats you have seen - this one might be different!

• Look at the headings / axis labels and units. What is the data showing?

• Identify the independent variable and the dependent variable. If possible, it’s helpful to label them “IV” and “DV”.

• What type of data is shown? Is it averages? Does it include a Range or Standard Deviation?

• Graphs: Check the axis labels. Have they plotted rate or time, mass/volume or concentration? Often students assume enzyme graphs have rate on the y axis - but sometimes they don’t!

• Tables: Check: is the Independent Variable in the first column? Is the data in each row consistent?
  
  

4. Look at the data
Now you understand its context, look at the actual dots or lines or numbers. Check:

• Does the Range overwhelm differences in values: Do the range bars or standard deviation bars overlap? If they do, then there is significant overlap between the populations of replicated results that were used to calculated the average values.

• Unspecified Ranges: If there are replicates but no range bars or standard deviation has been calculated, how broad does the range look when you compare the replicated data values to their mean?

• Trends: What trends can you observe? Then think about what principle of biology is being shown by the the trends.

Now think about what it all actually means:

• Values: How would you explain the highest value, the lowest value, the point at which the line crosses the x axis,

• Range: How would you explain the largest range? How would you change the method to reduce the spread in the data?
  
  

5. Ok - NOW look at the actual questions
Try to see past the detail. How does this data/question relate to things you have studied?

Your working memory can easily get overloaded with details, making it hard to think. If the examiners have introduced a new organism, its name won’t be important. What might be important is the environment in which it lives, or its interactions with other organisms. You know what data you have, and what the questions are, so pick out what actually matters here. Is this a question about enyme reaction rates? Or about surface area to volume ratio?

This is why it’s useful to look at the data first - you will be able to look at it with a clear eye, making it easier to pick out how it’s relevant to the material you have studied.

6. Give the required information
Avoid the common mistakes that lose students marks:

• If they say you should use the data, you must either quote it, or show how you have used in in a calculation

• Refer to the axis/data labels wherever possible. Don’t say “the graph goes up”, do say “the saturation of haemoglobin increases”

A-Level Biology Past Paper Graphs and Charts Exam Questions:

Got all that? Ok! Here are some questions for you to practice.

And remember - don’t read the questions until after you have made sense of the graph or chart.

This article was written by Dr Jenny Shipway with guidance and editing from Tom. Tom has over 26 years experience specialising in A level Biology teaching and tuition, and has helped many students achieve top grades in the subject.

Transport in Animals: Haemoglobin, Oxygen Dissociation Curves, and the Bohr Effect

Haemoglobin, Oxygen Dissociation Curves, and the Bohr Effect

Red blood cells stuffed full of haemoglobin. Their bright red colour tells us their haemoglobin is in the form of oxyhaemoglobin, with bound oxygen.

This article includes an explanation of the topic followed by a short multiple-choice quiz with answers, and a collection of past-paper A-level exam questions for you to try.

Single-celled organisms absorb oxygen directly from their surroundings for use in aerobic respiration. But animals have cells buried deep within their bodies, far from the outside world. For this reason, the ability to transport essential substances like oxygen, and to remove waste products like carbon dioxide, is crucial for all animals.

This A-level Biology topic is challenging, but it’s really important to build an understanding of the mechanisms behind these processes. You’ll need to understand exchange and transport, and get to grips with the role of haemoglobin in transporting oxygen and carbon dioxide. And you really will need to understand it properly - as with most A-level topics, memorisation is not enough.

The really clever bit about oxygen transport in animals is the way that cooperative binding affects haemoglobin’s oxygen dissociation curve. Master that and you’ll be well on your way to getting full marks in this topic.

Vocabulary:

1. Partial Pressure: The pressure exerted by one gas in a mixture.

2. Haemoglobin: A protein found in red blood cells. Able to bind oxygen, carbon dioxide, and other ligands.

3. Oxyhaemoglobin: Haemoglobin bound to oxygen, as occurs during oxygen transport.

4. Carbaminohemoglobin: Haemoglobin bound to carbon dioxide, as occurs during carbon dioxide transport. Yes it has a funny name! Be careful not to confuse it with carboxyhaemoglobin, which is hemoglobin bound with carbon monoxide.

5. Haemoglobinic Acid: Haemoglobin bound to a proton, as occurs during carbon dioxide transport.

6. Cooperative Binding: The phenomenon where the first oxygen molecule to bind to one of haemoglobin’s binding sites increases the affinity of the remaining binding sites for oxygen. And the first to release makes it easier for the others to release.

7. Carbonic Anhydrase: An enzyme that catalyses the reversible conversion of carbon dioxide and water into carbonic acid.

8. HCO3–: The bicarbonate ion, one of the ways in which carbon dioxide is transported in the blood.

9. Chloride Shift: The movement of chloride ions into red blood cells as bicarbonate ions move out, maintaining electrical neutrality during the transport of carbon dioxide.

10. Oxygen Dissociation Curve: A curve on a graph that shows how saturated with oxygen haemoglobin is at different partial pressures of oxygen. It curves because of the effect of cooperative binding. The position of the curve is affected by pH.

Partial Pressure:

None of this will make any sense if you don’t understand what partial pressure is, so that’s a good place to start. Partial pressure is the pressure exerted by one gas in a mixture. You can increase the partial pressure of oxygen molecules (O2) in air by either having greater air pressure, or by a larger proportion of the air being oxygen.

The percentage of Oxygen in the air is the same on Everest as at sea level.

• When you ascend Everest, the percentage of oxygen in the air does not fall, but the air pressure does. And so the partial pressure of oxygen in your alveoli falls.

• When you re-breathe the same air, the air pressure does not fall, but the percentage of oxygen in the air does. And so the partial pressure of oxygen in your alveoli falls.

Gases still have partial pressures when they are in solution. The partial pressure of carbon dioxide is really high in an unopened can of coke. And the partial pressure of oxygen in your body fluids must be carefully regulated if your cells are to survive.

Remember that oxygen is the final electron acceptor in oxidative phosphorylation on the inner mitochondrial membrane, where it becomes water (H2O). Respiration therefore removes oxygen molecules (O2) from the body, lowering its partial pressure. The harder a tissue works, the more ATP will be produced from aerobic respiration, and the more oxygen atoms will be moved from O2 into H2O.

Respiration therefore lowers the partial pressure of oxygen (O2) in the tissues. Especially in energy-hungry tissues like muscle.

The partial pressure of carbon dioxide (CO2) also changes in the body. Respiration produces carbon dioxide by decarboxylation of pyruvate in the link reaction and citrate (etc) in Krebs cycle. As the partial pressure of oxygen falls, that of carbon dioxide increases. It’s not the same oxygen atom (remember the one from O2 ended up in H20), but the two processes are closely connected.

Respiration therefore increases the partial pressure of carbon dioxide in the tissues. Especially in energy-hungry tissues like muscle.

This is why animals need a system to support gas transport - it is necessary to move oxygen in to the tissues from the outside world, and to move carbon dioxide out of the tissues to excrete it out of the body.

Haemoglobin’s role:

Haemoglobin plays a pivotal role in transporting oxygen and carbon dioxide in the bloodstream. Haemoglobin is a protein containing four polypeptide chains, each of which provides a binding site that can bind reversibly with oxygen or protons (and some other things too). The timing of its binding and release of its ligands depends on various factors:

Haemoglobin - there are four polypeptide chains, here two are shown in green, and two in red (apologies to anyone who is colour-blind, I didn’t make this graphic). Each polypeptide chain is folded to create a subunit of the protein, and each subunit provides a binding site which can bind one Oxygen molecule.

• Oxygen Binding: When oxygen levels are high, haemoglobin binds with oxygen molecules, forming oxyhaemoglobin. This happens in the lungs, where blood is brought close to the surface of the alveoli. Oxyhaemoglobin is bright red; this is what gives blood its red colour.

• Cooperative Binding: When the first oxygen molecule binds, haemoglobin changes shape in a way that increases the affinity of its remaining binding sites for oxygen. This results in a rapid increase in oxygen saturation once the first oxygen molecule binds to haemoglobin. There is a similar effect on release of oxygen - releasing one oxygen makes it easier for the others to be released.

• Carbon Dioxide Binding: Haemoglobin binds a small percentage of the carbon dioxide produced by the body tissues to help transport it back to the lungs. Haemoglobin bound to carbon dioxide is called carbaminohemoglobin, and is a dark maroon colour. It is not blue!
  
  
  

Carbon Dioxide transport:

About 30% of the carbon dioxide produced by body tissues gets directly bound by haemoglobin for transport. A lot more - about 70% - travels in the blood plasma. This is possible because of the action of the enzyme Carbonic Anhydrase.

• Carbonic Anhydrase: Inside the red blood cell, the enzyme carbonic anhydrase catalyses the reversible conversion of carbon dioxide and water into carbonic acid. This acid then dissociates into bicarbonate ions (HCO3-) and protons (H+).

• Haemoglobinic Acid: The positively-charged protons from the dissociated carbonic acid bind to the haemoglobin to form haemoglobinic acid. This keeps these positive charges inside the red blood cell.

• Chloride Shift: In contrast, the negatively-charged bicarbonate ions are free to diffuse out of the red blood cell into the blood plasma. To maintain electrical neutrality, chloride ions (Cl-) diffuse into the red blood cell. This is known as the chloride shift.
  
  
  

Cooperative Binding and the Oxygen Dissociation Curve:

The much-feared oxygen dissociation curve. The really interesting thing is that it is not a straight line. You need to know why not, and why this is crucial for oxygen delivery to the body tissues.

The Oxygen Dissociation Curve is a graph plotting the partial pressure of oxygen (how much oxygen there is in the environment) against how saturated the haemoglobin is with oxygen.

The graph is always drawn with the partial pressure of oxygen on the X-axis, showing low oxygen to the left, and high oxygen to the right. Oxygen binding is plotted against the Y-axis, with the curve plotted higher at partial pressures where the haemoglobin is more saturated with oxygen.

Take a little while to work out exactly what the graph is showing, as it can be a bit confusing at first.

As you might expect, when there is more oxygen around, more oxygen gets bound. But it’s not quite as simple as that.

The sigmoid shape of the oxygen dissociation curve shows why haemoglobin is so ideally suited to its role in oxygen transport. The shape of the curve is explained by haemoglobin’s remarkable property of cooperative binding.

Haemoglobin has four tertiary domains, each with its own binding site. So it can carry four oxygen molecules. The really clever bit is that when the first oxygen molecule binds, this causes a change of shape in the protein that increases the affinity of the other three binding sites for oxygen. This increased affinity increases their chances of binding oxygen too. This all has the effect that once just one oxygen has bound, the haemoglobin’s binding sites are quickly saturated. And the opposite happens when oxygen dissociates - the dissociation of the first oxygen reduces the affinity of the other binding sites.

The way in which one binding event encourages others is called Cooperative Binding. This ‘all or nothing’ tendency affects the shape of haemoglobin’s oxygen dissociation curve by squashing it down at the bottom and up at the top, creating its famous sigmoid shape.

The sigmoid shape of the oxygen dissociation curve is crucial for efficient oxygen delivery to tissues. At low oxygen concentrations (e.g., in tissues with high metabolic activity), haemoglobin exhibits low affinity for oxygen, allowing it to release oxygen to respiring cells. Conversely, at high oxygen concentrations (e.g., in the lungs), haemoglobin exhibits high affinity for oxygen, facilitating its uptake from the lungs.

The Bohr Effect: Carbon Dioxide and the Oxygen Dissociation Curve

Notice that the right-shifted, red curve is lower than the blue one. This tells us that at high CO2, haemoglobin has LESS affinity for oxygen. (The colours don’t mean anything.)

Haemoglobin’s oxygen dissociation curve isn’t fixed in place. It can move to different positions depending on the pH.

The pH in the red blood cell is affected by the partial pressure of carbon dioxide (remember how it behaves during transport?). High levels of carbon dioxide indicate that the body is active and needs more oxygen.

Active muscles also produce lactic acid through anaerobic respiration, which further reduces the pH.

A low (acidic) pH has the effect of moving the oxygen dissociation curve to the right. This means that any any given partial pressure of oxygen, this high-CO2, right-shifted curve is lower than before.

It’s not enormously intuitive, but you can see this clearly if you draw a line vertically up through the graph at a chosen partial pressure of oxygen. Look at where it meets each curve. It will hit the right-shifted curve before it hits the original curve, because the right-shifted, high-CO2 curve will have lower oxygen saturation at this (or any) patial pressure.

That means that at any partial pressure of oxygen, the high-CO2 haemoglobin has a lower affinity for oxygen than before, and is more likely to release its oxygen into the tissues.

Reducing haemoglobin’s affinity for oxygen at high partial pressures of carbon dioxide helps it release oxygen in the active tissues that need it most.

Fetal Haemoglobin and Myoglobin

Haemoglobin sometimes needs to pass its oxygen to other, similar oxygen-binding molecules. It needs to pass it to myoglobin for oxygen storage in muscles, and to fetal haemoglobin to pass oxygen to the growing foetus.

These similar-but-different molecules have their own oxygen dissociation curves. If oxygen is to be passed to them, they must have a higher affinity for oxygen than normal haemoglobin. And this is what is seen. When you look at their curves, they are left-shifted with respect to haemoglobin. Draw a line up from any chosen partial pressure of oxygen, and it will hit the curve for normal haemoglobin first, because the fetal haemoglobin or myoglobin will have higher oxygen saturation.

This means that at any partial pressure of oxygen, they have a higher affinity for oxygen, and are able to bind oxygen that has been released by the normal haemoglobin.

Multiple Choice Questions (answers below):

1. What is the primary function of haemoglobin in the bloodstream?
   a) Transporting nutrients
   b) Transporting oxygen
   c) Transporting waste products
   d) Transporting hormones
   

2. Which enzyme catalyzes the reversible conversion of carbon dioxide and water into carbonic acid?
   a) Carbon dioxide synthase
   b) Carbonic anhydrase
   c) Haemoglobinase
   d) Bicarbonate dehydrogenase
   

3. Which acid is formed when haemoglobin binds with a proton?
   a) Carbonic acid
   b) Haemoglobinic acid
   c) Hydrochloric acid
   d) Sulfuric acid
   

4. Which ions move into red blood cells when bicarbonate ions diffuse out?
   a) Sodium
   b) Potassium
   c) Chloride
   d) Hydrogen
   

5. What effect does an increase in carbon dioxide concentration have on the oxygen dissociation curve?
   a) It shifts the curve to the left
   b) It shifts the curve to the right
   c) It has no effect on the curve
   d) It decreases the steepness of the curve

Multiple Choice: answers

1. Answer: b) Transporting oxygen
2. Answer: b) Carbonic anhydrase
3. Answer: b) Haemoglobinic acid
4. Answer: c) Chloride
5. Answer: b) It shifts the curve to the right

How did you do?

These questions were just a quick test to see if you can remember some of the key points. If you struggled a bit then go back and review the content. But also check that you really understand what’s going on with this topic. The exam board will intentionally phrase the questions to make it as difficult as possible for anyone to answer by having just memorised key facts.

When you’re ready, try some real exam questions:

This article was written by Dr Jenny Shipway in collaboration with Tom