Each actin (thin) filament is made of two ‘F’ (filamentous) actins helically wound to each other. Each ‘F’ actin is a polymer of monomeric ‘G’ (Globular) actins. Two filaments of another protein, tropomyosin also run close to the ‘F’ actins throughout its length. A complex protein Troponin is distributed at regular intervals on the tropomyosin. In the resting state a subunit of troponin masks the active binding sites for myosin on the actin filaments (Figure 3a).
Each myosin (thick) filament is also a polymerised protein. Many monomeric proteins called Meromyosins (Figure 3b) constitute one thick filament. Each meromyosin has two important parts, a globular head with a short arm and a tail, the former being called the heavy meromyosin (HMM) and the latter, the light meromyosin (LMM). The HMM component, i.e.; the head and short arm projects outwards at regular distance and angle from each other from the surface of a polymerised myosin filament and is known as cross arm. The globular head is an active ATPase enzyme and has binding sites for ATP and active sites for actin.