Young myofibers contain a 7:1 ratio of thin to thick filaments.

The sarcomeres are composed of thin and thick filaments.

Muscle fibers are arranged in a linear fashion with cross bridges between thin and thick filaments.

Sarcomeres are the basic contractile units which consist of thin and thick filaments.

It is found in the thick filaments of sarcomeres(myosin).

All of these roles require myosin II to be in the form of thick filaments.

Thick filaments consist primarily of the protein myosin.

Invertebrate thick filaments are thought to be composed of an inner paramyosin core surrounded by myosin.

This increase in distance allows thick filaments to fit in between and interact, enabling deformation or contraction.

Myosin filaments, the thick filaments, are bipolar and extend throughout the A-band.

The ability to form thick filaments is regulated by phosphorylation of three threonines near the tail of the long coiled-coil.

I-band is the zone of thin filaments that is not superimposed by thick filaments.

For a model system, we have focused on the dynamics of myosin II thick filaments in D. discoideum .

Physiologically, this contraction is not uniform across the sarcomere; the central position of the thick filaments becomes unstable and can shift during contraction.

Muscle contraction is caused by the sliding action of the thick filaments over the thin filaments of the myofibril.

Force is generated in striated muscle by the interactions between myosin thick filaments and actin thin filaments.

In muscle cells, the long coiled-coil tails of the individual myosin molecules join together, forming the thick filaments of the sarcomere.

These proteins are organized into thin filaments and thick filaments, which repeat along the length of the myofibril in sections called sarcomeres.

Thin filaments are actin filaments, whereas thick filaments consist of an arrangement of myosin proteins.

This dimension is consistent with myosin II thick filaments measured from the in vitro electron microscopy photographs [ 29 ] .

When the protein is fully phosphorylated, it remains largely in the monomeric state; whereas removal of these phosphates allows the protein to assemble into thick filaments.

Myosin, the actin motor protein, has an extended coiled-coil domain necessary for the assembly of the muscle thick filaments [ 7 ] .

There are two types of filaments: actin (thin filaments) and myosin (thick filaments) which are arranged in parallel.

These proteins are thought to be involved in anchoring the thick filaments of the sarcomere (myosin) to other filaments, namely titin, stabilizing and aligning the structure.

These have been shown to align to the 43 nm axial repeats of myosin thick filaments with immunoglobulin domains correlating to myosin crowns.