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Cambridge International A Level Biology Revision Guide

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Chapter 15: Coordination<br />

Structure of thick and thin filaments<br />

Thick filaments are composed of many molecules of<br />

myosin, which is a fibrous protein with a globular head.<br />

The fibrous portion helps to anchor the molecule into the<br />

thick filament. Within the thick filament, many myosin<br />

molecules all lie together in a bundle with their globular<br />

heads all pointing away from the M line.<br />

The main component of thin filaments, actin, is a<br />

globular protein. Many actin molecules are linked together<br />

to form a chain. Two of these chains are twisted together<br />

to form a thin filament. Also twisted around the actin<br />

chains is a fibrous protein called tropomyosin. Another<br />

protein, troponin, is attached to the actin chain at regular<br />

intervals (Figure 15.28).<br />

M line<br />

How muscles contract<br />

Muscles cause movement by contracting. The sarcomeres<br />

in each myofibril get shorter as the Z discs are pulled closer<br />

together. Figure 15.28 shows how this happens. It is known<br />

as the sliding filament model of muscle contraction.<br />

The energy for the movement comes from ATP<br />

molecules that are attached to the myosin heads. Each<br />

myosin head is an ATPase.<br />

When a muscle contracts, calcium ions are released<br />

from stores in the SR and bind to troponin. This stimulates<br />

troponin molecules to change shape (Figure 15.28).<br />

The troponin and tropomyosin proteins move to a<br />

different position on the thin filaments, so exposing<br />

parts of the actin molecules which act as binding sites for<br />

1 When the muscle is relaxed,<br />

tropomyosin and troponin<br />

are sitting in a position<br />

in the actin filament that<br />

prevents myosin from<br />

binding.<br />

tropomyosin<br />

actin<br />

troponin<br />

347<br />

2 When muscle contraction<br />

starts, the troponin and<br />

tropomyosin change shape to<br />

allow myosin heads to bind to<br />

actin.<br />

myosin head<br />

3 Myosin heads tilt, pulling<br />

the actin and causing the<br />

muscle to contract by<br />

about 10 nm.<br />

4 ATP hydrolysis causes<br />

the release of myosin<br />

heads. They spring back<br />

and repeat the binding<br />

and tilting process.<br />

Figure 15.28 The sliding filament model of muscle contraction.

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