Imaging from nearly 100,000 electron microscopic images has shown an ingenious way to turn off the myosin protein to conserve energy. He is involved in muscle activity. Details of the study are reported by the journal Nature.
Myosin interacts with other proteins and molecules to move a person. It sits within muscle fibers, forming long myosin filaments made up of hundreds of individual protein molecules. When muscle activity stops, the formation of myosin filaments goes in the opposite direction: filaments return to the myosin molecule’s individual state.
Visualization, developed by scientists from the University of Leeds in the UK and the University of East Carolina in the United States, showed how the molecule changes in this case. It folds up and becomes more compact.
A single myosin molecule consists of a “head” and a “tail.” In the active state, the tails of the molecules combine to form fibrous myosin filaments. The heads inside the filament bind to another protein, actin, to contract the muscles.
After examining 96 thousand images obtained using an electron microscope, the scientists saw how the myosin molecule takes an inactive form with unprecedented detail. The tail of each molecule is wrapped around the head and locked in place. This process stops the activity of myosin and makes it easier to transport it in the human body.
Scientists have known for decades about the role of myosin in muscle activity. But until now, it was not clear to them exactly how he passed into an inactive state or how his formation was so strictly controlled.