Antagonistic Pairs

What you need to know (from the AQA specification)

Muscles act in antagonistic pairs against an incompressible skeleton.

The first key concept to understand is that muscles work in antagonistic pairs. The word antagonist means ‘a person who opposes the other’, and muscle pairs work in this way, as they oppose each other.

We are going to look at a bicep curl to see how this works. Here, the group of antagonistic muscle pairs includes the biceps & triceps. Other structures to be aware of:

  • Tendons — connect muscles to bones, allowing movement of the skeleton (e.g. lifting the arm). You may have heard of tendonitis, a common sports injury (e.g. Achilles tendonitis). The suffix ‘itis’ means inflammation, so tendonitis means inflammation of a tendon.
  • Ligaments — connect bone to bone, providing stability at joints. A common sports injury is tearing the anterior cruciate ligament (ACL) in the knee.

Bicep Curl Example

  • Pulling the lower arm upwards:
    • When the bicep contracts (this is known as the agonist), the tricep does the opposite and relaxes (this is called the antagonist), so the lower arm is pulled upwards.
  • Pulling the lower arm downwards:
    • When the tricep contracts (this time it’s the agonist), the bicep relaxes (the antagonist) and the lower arm is pulled downwards.

Does this work for other muscle pairs? Absolutely! There are many examples: quadriceps and hamstrings can pull the leg upwards or downwards.

Important

Due to how muscles are structured, they pull; they do NOT PUSH.

Structure of Muscles

What you need to know (from the AQA specification)

Gross and microscopic structure of skeletal muscle. The ultrastructure of a myofibril.

Let’s continue with the bicep curl as an example, and try to understand what is happening at a structural level that is causing the muscle to contract.

High Level Organisation

  • Skeletal muscle is a highly organized tissue.
  • Muscles are made of bundles, called fascicles (which are encased and separated by layers of connective tissue)
  • These fascicles are made of muscle fibres (again muscle fibres are separated from each other by connective tissue)
  • These muscle fibres are made of myofibrils

A single muscle fibre contains hundreds to thousands of myofibrils. Interestingly, if you are more trained (i.e. you have done more bicep curls) you can have more myofibrils than someone who hasn’t hit the gym in a while.

Myofibrils are made of sarcomeres which are repeating units and the basis of muscle contraction. When these sarcomeres contract, the entire muscle contracts.

Muscle Fascicle -> Muscle FibreMyofibril
Skeletal muscle made of bundles (fascicles) of muscle fibresMuscle fibre containing myofibrils made of repeating sarcomeres

Images adapted from OpenStax College, via Wikimedia Commons (CC BY 4.0).

Muscle Fibre Structures

  • Sarcolemma: the membrane surrounding the entire muscle fibre (not individual myofibrils).
  • Sarcoplasm: cytoplasm of muscle cells, which contains other structures (e.g. sarcoplasmic reticulum, nuclei)
  • Nuclei: the muscle fibre contains many nuclei, allowing high rates of protein synthesis for actin and myosin.
  • Mitochondria: required for ATP production, which is especially important for muscle contraction.
  • T-tubules: deep infoldings of the sarcolemma that transmit action potentials to the sarcoplasmic reticulum.
  • Sarcoplasmic reticulum: controls calcium release, and calcium triggers muscle contraction.
T-tubule structure in muscle fibre
Image by Blausen Medical Communications, via Wikimedia Commons (CC BY 3.0)

You’ll see how the sarcolemma, T-tubules and sarcoplasmic reticulum work together at the neuromuscular junction below, and on the Synaptic Transmission page.

Ultrastructure of Myofibril

Our understanding of muscles came from observing myofibrils under a microscope.

Scientists observed 2 main protein filaments actin (thin filament) and myosin (thick filament).

The animation below shows you an example of 1 sarcomere unit, but in reality there are many repeating sarcomeres. You need to be aware of the following lines/bands (Note: these can be quite challenging to remember!)

  • M lines — denote the middle (M for middle) of the sarcomere and provide attachment points for myosin filaments
  • Z lines — outline the boundaries of the sarcomere
  • I bands — contain actin only. Because there is a single filament present, this region appears lighter under a microscope
  • A band — the length of the myosin filaments. It includes the regions where actin and myosin overlap, which appear darker because two filaments are present
  • H zone — contains myosin only. This region appears lighter under a microscope because only one filament is present

What happens to these bands when the muscle contracts?

  • Z lines moved closer together (this shows that the sarcomere has shortened).
  • I bands (actin only) have shortened
  • H zone (myosin only) has shortened
  • A band (actin & myosin) remains unchanged.

Important

  • Actin and myosin filaments are sliding over each other when the muscle contracts. Actin and myosin are not shortening. Only the sarcomere has shortened.
  • Regions which appear darker under a microscope have 2 filaments (e.g. where actin and myosin overlap). Regions which appear lighter have only 1 filament (e.g. I band/H zone)

Neuromuscular Junction

What stimulates the muscles to contract?

Let’s look at the neuromuscular junction to show how the release of calcium controls this and how muscle contraction is brought about.

Note: There is a separate topic, Synaptic Transmission, which goes into more detail on synapses. I’m outlining it here as it relates to muscle contraction.

Sliding Filament Theory

What you need to know (from the AQA specification)

The roles of actin, myosin, calcium ions and ATP in myofibril contraction. The roles of calcium ions and tropomyosin in the cycle of actinomyosin bridge formation. (The role of troponin is not required.)

Now let’s look in more detail as to how this sarcomere contracts, specifically the sliding filament mechanism.

Steps in Sliding Filament Theory

  1. Actin-myosin binding sites are blocked: When muscle is resting the tropomyosin has blocked actin-myosin binding sites, which means that myosin can’t bind to actin and muscle contraction can’t happen.
  2. But, when the calcium is released from sarcoplasmic reticulum (what we just looked at in neuromuscular junctions) it binds to troponin. This causes the tropomyosin to change positions exposing the actin-myosin binding sites.
  3. The myosin heads can now bind to actin, and a cross bridge is formed.
  4. Next, the myosin heads perform a power stroke which pulls the actin filaments towards the centre of the sarcomere, releasing ADP and Pi (you can see on the animation that the sarcomere has shortened)
  5. Next, ATP binds to the myosin head and causes it to detach from actin.
  6. ATP hydrolysis then occurs releasing energy to re-cock the myosin head back to original position, so that the cycle can continue.

What happens if there is no ATP?

Rigor mortis is a condition where there isn’t any ATP, so the myosin heads remain attached to the actin, locking the muscle fibres in a contracted position.

Does this cycle keep repeating itself? When does it stop?

  • This cycle can continue assuming the muscle fibre is continuously stimulated by nerve impulses.
  • As this will trigger the ongoing release of calcium ions from the sarcoplasmic reticulum (think back to the neuromuscular junction)
  • The cycle stops when the muscle fibre is not stimulated and calcium returns back to the sarcoplasmic reticulum via active transport, which requires ATP.

Role of ATP & Phosphocreatine

What you need to know (from the AQA specification)

The roles of ATP and phosphocreatine in muscle contraction.

Role of ATP in Muscle Contraction

  1. The hydrolysis of ATP provides energy to re-cock the myosin head back into the high-energy position, which then drives the power stroke, pulling the actin filaments towards the centre of the sarcomere

  2. ATP is needed to detach the actinomyosin bridge and re-set the myosin head back to its starting position.

  3. Finally, it’s responsible for active transport of calcium ions to return to sarcoplasmic reticulum, when the muscle is relaxed.

(Note: ‘Actinomyosin bridge’ is the term used directly from the AQA specification. It means the link between myosin and actin and is often referred to as ‘cross-bridge’.)

What are the sources of ATP?

We’ve just seen how important ATP is for muscle contraction, but how is it made?

There are 3 main sources of ATP:

Aerobic respiration requires oxygen and takes a lot longer to produce ATP, making it unsuitable for quick short bursts of high intensity exercise (e.g. sprinting from a lion, because that is a regular occurrence!).

High intensity exercise is fuelled partially by glycolysis and by phosphocreatine which is stored in muscles.

Aerobic RespirationAnaerobic RespirationPhosphocreatine
Oxygen requiredNo oxygen needed
Lactate is produced
No oxygen needed
Phosphocreatine + ADP ⇌ Creatine + ATP
Produces a lot of ATP (~32 ATP)Produces much less ATP than aerobic (~2ATP)(~1ATP)
Produces ATP at slower rateProduces ATP at a fast rateRegenerates ATP very rapidly
Low intensity exerciseHigh intensity exercise
(1-3 mins)
Very high intensity short burst
< 10 seconds

Phosphocreatine

  • Is a phosphorylated form of creatine, stored in the muscles.
  • It is used to rapidly regenerate ATP for high intensity exercise (e.g. short sprints, 100m)

Phosphocreatine

Phosphocreatine donates a phosphate group to ADP to form ATP and creatine.

Phosphocreatine + ADP ⇌ Creatine + ATP

  • It’s a reversible reaction, and the stores of phosphocreatine become replenished during rest.
  • Interestingly
    • Some people take creatine supplements to help increase stores of phosphocreatine, to improve their performance at very high-intensity exercise.
    • If you wanted to train your phosphocreatine system (i.e. high-intensity/short sprints) it’s important to take long enough rests in between sprints to ensure you can replenish your phosphocreatine stores

Slow & Fast Twitch Muscle Fibres

What you need to know (from the AQA specification)

The structure, location and general properties of slow and fast skeletal muscle fibres.

There are two main types of muscle fibres: Slow & Fast Twitch.

These exist in different proportions across individuals and across different types of muscles.

For example, sprinters often have a higher proportion of fast twitch muscle fibres than ultramarathon runners. The relative proportions also vary depending on the location of the muscle in the body (e.g. calf muscles often have a higher proportion of slow twitch muscles as they need to be able to withstand continuous muscle contraction).

Slow Twitch

Function

  • Contract more slowly than fast twitch
  • Less powerful contractions over a long period of time
  • Used for longer sustained endurance activities

Structural adaptations

  • More myoglobin (protein that acts as an oxygen store, appears bright red)
  • More mitochondria for aerobic respiration to produce more ATP
  • Rich supply of blood vessels to deliver oxygen and glucose for aerobic respiration
  • High resistance to fatigue (relies on aerobic respiration, generates large amounts of ATP)

Fast Twitch

Function

  • Contract quickly
  • More powerful contractions over a short period of time
  • Used for shorter, higher intensity activities

Structural adaptations

  • Larger (thicker) fibres, so they are able to generate powerful contractions
  • High stores of phosphocreatine
  • High stores of glycogen
  • Fatigues quickly (relies on anaerobic respiration, lactate is produced)

Structure & Function linkage

Try to think about how the structure can enable the function. E.g. fast twitch fibres need to contract quickly and forcefully, so a structure that could support that would be larger (thicker) fibres

How this topic is tested

This analysis is based on past paper data from 2017 to 2025. It is intended for interest only and is not predictive of what will appear in future papers.

  • Tested in 5 of 9 years (2017–2025): 17 question parts worth 46 marks.
  • 22nd most-examined topic overall by marks, 4th in Unit 6.

Marks by year

2017
4 marks
2018
0 marks
2019
7 marks
2020
14 marks
2021
0 marks
2022
0 marks
2023
8 marks
2024
13 marks
2025
0 marks

Most-tested spec points

  • Slow & Fast Skeletal Muscle Fibres: tested in 4 parts (15 marks)
  • The Mechanism of Muscle Contraction: tested in 4 parts (10 marks)
  • ATP & Phosphocreatine in Contraction: tested in 2 parts (6 marks)
  • Structure of Skeletal Muscle & the Myofibril: tested in 2 parts (5 marks)

Also links to: Required Practical 11, Blood Glucose & the Role of the Liver, The Link Reaction & Krebs Cycle.

Maths and practical skills

  • Colorimeter or potometer measurements (AT b): e.g. 2020 P2 Q4.3
  • Units and standard form (MS 0.1, 0.2): e.g. 2024 P2 Q2.1
  • Averages (MS 1.6): e.g. 2024 P3 Q4.2
  • Glassware and serial dilutions (AT c): e.g. 2020 P2 Q4.2
  • Percentages, ratios and fractions (MS 0.3): e.g. 2024 P2 Q2.1
  • Tables, bar charts and histograms (MS 1.3): e.g. 2017 P2 Q3.4
  • Using equations (MS 2.2): e.g. 2017 P2 Q3.3
  • Area, volume and surface area of shapes (MS 4.1): e.g. 2017 P2 Q3.3

Tips from examiner reports

What students commonly get wrong
  • Know which filaments are in each bandWatch out: explain the bands by the filaments they contain. I band = actin only, H zone = myosin only, and the darkest region = where actin and myosin overlap (part of the A band). 2020 P2 Q4.1
  • Binding site, not active siteWatch out: tropomyosin blocks the myosin binding sites on actin. Don't call them "active sites"; that's enzyme terminology. 2019 P2 Q4.2
  • Say "myosin head", not "myofibril"Watch out: ATP breaks the actinomyosin bridge and moves the myosin head. Write "myosin", not "myofibril", and mention the head. 2023 P2 Q10.1
  • Compare both fibre typesWatch out: when a question asks about fast and slow fibres, compare both, e.g. fast fibres contract quickly, whereas slow fibres contract slowly. 2024 P2 Q2.3
  • Muscles contract and relaxWatch out: describe muscles as contracting and relaxing, not "constricting", "expanding" or "lengthening". 2020 P2 Q1.1

Practise with the exam questions below ↓

Exam Question Practice

Roles of ATP in muscle contraction

A sprinter’s leg muscles use ATP very quickly during a race.

Describe three roles of ATP in muscle contraction.

(3 marks)

Hint

What has to happen to the cross-bridge before myosin can bind again? What resets the myosin head? What happens to calcium ions when the muscle relaxes?

Mark Scheme

Max 3 marks

  1. ATP is used to break the actinomyosin cross-bridge (detach myosin from actin) (1 mark)
  2. ATP is used to move the myosin head back (recock it) (1 mark)
  3. So the actin filaments are pulled along in the next power stroke (1 mark)
  4. ATP is used for the active transport of calcium ions back into the sarcoplasmic reticulum (1 mark)

Explanation (not marked): ATP binds to the myosin head and breaks the cross-bridge. Its hydrolysis releases energy that moves the head back, ready to bind further along the actin. When the muscle relaxes, calcium ions are pumped back into the sarcoplasmic reticulum by active transport, which also uses ATP.

Also accepted / rejected

Also accepted

  • “To form actinomyosin”, or “to attach or detach myosin and actin” (point 1)
  • “To change the shape of the myosin head” (point 2)

Not accepted

  • “Active site” (point 1, as it’s a binding site)
Tips
  • ATP breaks the actinomyosin cross-bridges. Write “myosin”, not “myofibril”
  • ATP moves the myosin head (include “head”), which pulls the actin
  • ATP is also used to actively transport calcium ions back into the sarcoplasmic reticulum
  • Call it a binding site, not an active site
Glycogen in fast and slow fibres

Scientists took small samples from the leg muscles of sprinters and of long-distance runners. The sprinters’ samples contained mostly fast muscle fibres. They had a higher concentration of glycogen than the long-distance runners’ samples, which contained mostly slow muscle fibres.

Explain how this difference in glycogen concentration is related to the different properties of fast and slow muscle fibres.

(4 marks)

Hint

How quickly does each type of fibre contract, and for how long? Which type of respiration does each mainly use, and how much ATP does that give per glucose? Where does the glucose come from?

Mark Scheme
  1. Fast fibres contract quickly but slow fibres contract slowly, or fast fibres are used for short periods but slow fibres for long periods (1 mark)
  2. Fast fibres mainly use anaerobic respiration, or slow fibres use aerobic respiration (1 mark)
  3. Fast fibres produce ATP quickly, or anaerobic respiration gives less ATP per glucose than aerobic respiration (1 mark)
  4. Glycogen is a store of glucose, which is hydrolysed to glucose (glycogenolysis) (1 mark)

Explanation (not marked): Fast fibres contract quickly, in short bursts such as sprinting. They mainly respire anaerobically, which makes ATP quickly but gives only a little ATP from each glucose. So they use up glucose fast, and they keep a large store of it as glycogen. Slow fibres contract slowly over long periods. They respire aerobically, which gives much more ATP from each glucose, so they need less stored glycogen.

Also accepted / rejected

Also accepted

  • Examples such as sprinting (short) and marathon running (long) (point 1)
  • “Release energy” for produce ATP (point 3)

Not accepted

  • “Produce energy” (point 3)
Tips
  • Compare both fibre types in each point, for example fast fibres contract quickly whereas slow fibres contract slowly
  • Say fast fibres use anaerobic respiration. “Work anaerobically” isn’t accepted
  • Link to ATP. Fast fibres produce ATP quickly, and anaerobic respiration gives less ATP per glucose. Energy is released, not “produced”
  • Glycogen is a store of glucose that is hydrolysed to glucose (glycogenolysis). Don’t confuse this with glycolysis or glycogenesis
Creatine supplements and carbohydrate loading

A 100 m sprinter takes creatine supplements during training. A marathon runner eats extra carbohydrate for a few days before a race, which is called carbohydrate loading.

Describe and explain how each of these can improve the performance of the type of muscle fibre used most in each race.

(5 marks)

Hint

Which type of fibre does each race mainly use? What does creatine become in muscle, and how does that help with ATP? What happens to the extra carbohydrate, and how is it used later?

Mark Scheme

Max 5 marks. No more than 3 marks can come from points 3 to 7.

Muscle fibres

  1. Fast fibres are used in short, intense exercise, such as a sprint (1 mark)
  2. Slow fibres are used in long exercise, such as a marathon (1 mark)

Creatine

  1. Creatine is used to make phosphocreatine (1 mark)
  2. Phosphocreatine provides phosphate to ADP to make ATP quickly (1 mark)

Carbohydrate loading

  1. The extra carbohydrate is stored as glycogen (glycogenesis) (1 mark)
  2. Glycogen is hydrolysed to glucose (glycogenolysis) (1 mark)
  3. The glucose is used in respiration to make ATP (1 mark)
Also accepted / rejected

Also accepted

  • “Fast-twitch” and “slow-twitch” fibres (points 1 and 2)
  • “Glycolysis” for respiration (point 7)
Tips
  • Link the fibre type to the exercise. Fast fibres are used for short, intense exercise and slow fibres for long exercise, not “aerobic” or “anaerobic exercise”
  • Creatine forms phosphocreatine, which gives phosphate to ADP to make ATP. Write phosphocreatine in full
  • Carbohydrate is stored as glycogen (not starch), which is hydrolysed to glucose for respiration
  • Don’t confuse glycogen with glucagon, or mix up glycogenesis, glycogenolysis and glycolysis

More questions on this topic in Exam Practice →