Structure of Contractile Proteins
The structure of contractile proteins, specifically actin and myosin, is critical for muscle contraction. Actin, the thin filament, is composed of two helically-wound strands of F-actin, which is itself a polymer of monomeric G-actin. Surrounding the F-actin are two strands of tropomyosin, extending throughout its length. At intervals on these tropomyosin strands, a protein called troponin is found. In the resting state, a subunit of troponin blocks the active binding sites on actin for myosin.
On the other hand, myosin, the thick filament, consists of polymerized proteins known as meromyosins. Each meromyosin has a globular head and a tail. The head, referred to as heavy meromyosin (HMM), contains ATPase activity and binding sites for both ATP and actin. During muscle contraction, these proteins interact in a cycle that involves the sliding of actin over myosin, which is essential for muscle dynamics.