The cytoskeleton and its many molecular motors are major players in a variety of cellular functions. The interconnected networks of cytoskeletal filaments act as tracks directing molecular motor transport and provide structural support and organization to cells. One example of a class of motor proteins is the myosin superfamily, a large family of proteins whose members are involved in diverse cellular processes, including cellular transport, migration and structure maintenance. A dimeric myosin motor is capable of processive ATP-dependent hand-over-hand motion employing actin filaments as tracks.
The stepping mechanics of molecular motors are force-dependent (pN), nanoscopic (1-100 nm) and often very fast (∼1-100 Hz). Thus, the investigation of discrete steps and the subsequent mechanics of myosin motion on actin demands the use of high-resolution optical tweezers. With LUMICKS’ C-Trap™, it is possible to observe myosin activity, the processive motion, the binding kinetics along actin, and to determine its thermodynamic properties at the single-molecule level.