Dictyostelium discoideum is a slime mould that expresses several myosin isoforms, including a myosin II that has very similar ATPase properties of that from vertebrate skeletal muscle. It is possible to exploit molecular biological methods to introduce mutations into the myosin motor domain in order to study structure-function relationships. The motor domain contains 4 tryptophan residues, one of which at position W501 (shown in yellow space fill) shows a large fluorescence change when the C-terminal domain rotates on hydrolysis of ATP. This conformational change can be monitored using rapid-reaction methods such as stopped-flow and temperature-jump.

• Malnasi-Csizmadia et al 2000

• Malnasi-Csizmadia et al 2001

• Conibear et al 2004

• Kintses et al 2007