Structure of the vertebrate skeletal muscle is quite complicated. The muscle is made up of many fibers. Each fiber contains many myofibrils. Each myofibril is divided into individual cells, the so-called sarcomeres, which are arranged end to end along its length. Each sarcomere contains the myofilaments, thick and thin, that are based on, respectively, myosin and actin. Interaction between the proteins coupled with the ATP hydrolysis is a prerequisite of the muscle contraction usually observed on the level of fibers.
Representation of the new way of the myosin molecule packing into the vertebrate skeletal muscle thick filament on the basis of which the complete, bipolar structure (the so-called CB model) has been computed. It is introduced the twisted myosin, instead of straight, and asymmetrical cross-bridge crown, instead of symmetrical. The filament looks as being two-stranded, but has threefold rotational symmetry.
The so-called cross-bridge zone of the thick filament is represented. The left and right filaments are computed on the basis of the cross-bridge crown configurations denoted in table as the 1M and 4E, respectively.
