The molecular demon switches mainly between two conformations. The first, or basic state, upon recognizing and binding the ligand or substrate following an induced fit, undergoes a change in conformation which leads to the second quasi-stable state: the protein-ligand complex. In order to reset the protein to its original, basic state, it needs ATP. When ATP is consumed or hydrolyzed, the ligand is released and the demon acquires again information reverting to its basic state. The cycle may start again.