A spectrofluorimetric study of the interaction of myosin with ATP

Formation of the enzymatically active rnyosin-ATP complex produces a reversible change in the fluorescence of the tryptophan residues, which may be interpreted in terms of a structural rearrangement causing the tryptophan to enter a more hydrophobic environment. Fluorescence is used to follow the kinetics of the formation and decomposition of the enzyme-substrate complex.