Skeletal muscle is striated with fast and slow twitch fibres
Cardiac muscle, unlike skeletal, is involuntary
Smooth muscle is non striated and is under involuntary control, often forming a ring to contract
Myofibrils make up muscle fibres, each contains many sarcomeres making up the striated muscle with light and dark bands
A sarcomere consists of myosin - the thicker protein filament, and actin - the thinner protein filament
The Z line marks the end of a sarcomere
The I band is isotropic and light due to only having actin
The A band is anisotropic and is dark as it is made of both myosin and actin filaments
The H zone is the centre of the sarcomere made of only myosin
There are many ATP in the sarcoplasm of a sarcomere as it is needed to detach myosin heads from the actin filaments
When the sarcomere contracts, the I band gets smaller and the A band gets larger, the H band stays the same size
Slow twitch fibres contract more slowly than fast twitch
Slow twitch muscle fibres have less glycogen stores than fast twitch
Slow twitch muscle fibres do aerobic respiration and fast twitch do anaerobic respiration due to only being used for short bursts of energy
Slow twitch fibres are more red due to a better blood supply than fast twitch fibres as they need oxygen for aerobic respiration
Slow twitch fibres are also redder in colour due to myoglobin, which stores oxygen in the muscles for aerobic respiration
An action potential arrives at the neuromuscular junction and calcium ions diffuse into the synaptic knob causing vesicles of acetylcholine to fuse with the membrane, releasing it
After sodium ions diffuse across the sarcolemma, depolarising it, Ttubules carry the action potential deep into the sarcomere, calcium ions are released from the sarcoplasmic reticulum
T tubules are extensions of the sarcolemma allowing action potentials to travel deep into the fibre
After calcium ions diffuse from the sarcoplasmic reticulum, they move the tropomyosin binding the actin, revealing the myosin head binding site
Myosin heads bind to the exposed myosin binding site on actin, ADP + Pi are released from the myosin head causing it to bend, pulling the actin toward the centre of the sarcomere
ATP binding to the myosin head will release it from the myosin binding site on the actin, separating it from the actin, ATP's hydrolysis by ATPase will cause the myosin head to return to its original position, allowing it to bind to the next exposed binding site, moving the actin toward the centre of the sarcomere
ATP can be supplied to skeletal muscle by anaerobic and aerobic respiration, phosphocreatine is also found in the sarcoplasm, phosphates are stored that can quickly be attached to ADP during intense exercise, creatine is replenished when an organism is at rest
Antagonistic muscles are how the skeleton moves, muscles work against each other in antagonistic pairs to extend each muscle in turn
Antagonistic pairs can both be contracted at once to provide rigidity, supporting the posture and skeleton
Muscles are attached to the skeleton by tendons
Smaller contractions require fewer fibres so less are stimulated, larger contractions require a larger mass of fibres so more action potentials are sent to more fibres
ATP becoming ADP + Pi causes the power stroke where myosin heads move toward the centre of the sarcomere
Calcium ions diffuse from the sarcoplasmic reticulum when an action potential arrives
Calcium ions activate ATPase for ATP hydrolysis for the power stroke