The Sliding Filament Theory
Structure of thick & thin filaments in a myofibril
- The thick filaments within a myofibril are made up of myosin molecules
- These are fibrous protein molecules with a globular head
- The fibrous part of the myosin molecule anchors the molecule into the thick filament
- In the thick filament, many myosin molecules lie next to each other with their globular heads all pointing away from the M line
- The thin filaments within a myofibril are made up of actin molecules
- These are globular protein molecules
- Many actin molecules link together to form a chain
- Two actin chains twist together to form one thin filament
- A fibrous protein known as tropomyosin is twisted around the two actin chains
- Another protein known as troponin is attached to the actin chains at regular intervals
How muscles contract - the sliding filament theory
- Muscles cause movement by contracting
- During muscle contraction, sarcomeres within myofibrils shorten as the Z discs are pulled closer together
- It is not the filaments that contract as the myosin and actin molecules remain the same length
- Myosin and actin filaments slide over one another
- This is known as the sliding filament theory of muscle contraction and occurs via the following process:
- An action potential arrives at the neuromuscular junction (a specialised synapse between a motor neuron nerve terminal and its muscle fibre)
- Calcium ions are released from the sarcoplasmic reticulum (SR)
- Calcium ions bind to troponin molecules, stimulating them to change shape
- This causes troponin and tropomyosin proteins to change position on the actin (thin) filaments
- Myosin binding sites are exposed on the actin molecules
- The globular heads of the myosin molecules bind with these sites, forming cross-bridges between the two types of filaments
- Myosin heads bend, pulling the actin filaments towards the centre of the sarcomere and causing the muscle to contract a very small distance; this bending of the myosin heads is known as the power stroke
- ATP plays an important role in this process
- The binding of ATP to the myosin heads produces a change in shape of the myosin heads that allows them to detach from the actin filaments
- The enzyme ATPase hydrolyses ATP into ADP and inorganic phosphate which causes the myosin heads to move back to their original positions, this is known as the recovery stroke
- The myosin heads are then able to bind to new binding sites on the actin filaments, closer to the Z disc
- The binding of the myosin heads to their new binding site causes the release of ADP and phosphate and results in a new power stroke
- The myosin heads move again, pulling the actin filaments even closer to the centre of the sarcomere, causing the sarcomere to shorten once more and pulling the Z discs closer together
- ATP binds to the myosin heads once more in order for them to detach again
- As long as troponin and tropomyosin are not blocking the myosin-binding sites and the muscle has a supply of ATP, this process repeats until the muscle is fully contracted
The sliding filament theory of muscle contraction
- Once muscle stimulation stops, calcium ions leave their binding sites on troponin molecules
- They are actively transported back to the SR
- Without calcium ions bound to them, the troponin molecules return to their original shape
- This pulls the tropomyosin molecules in a position that blocks the actin-myosin binding sites
- Since no cross bridges can form between actin and myosin, no muscle contraction can occur
- The sarcomere will lengthen again as actin filaments slide back to their relaxed position
Examiner Tip
There is a lot to remember here so take some time to go through it and ensure you understand the order of events.
Because muscles require a source of ATP for myosin heads to detach (and the muscle to stop contracting) this explains rigor mortis (stiffening of the joints and muscles of a body a few hours after death) as there is no ATP after death to detach the myosin heads, the muscles remain contracted!