Cell motors wobble to binding sites

摘要

Improved high-speed imaging of single molecules shows protein motors use random motions to clamber towards their targets. When muscles contract or cells divide, the necessary movements depend on foot-like projections of the protein myosin 'stepping' their way to binding sites on strands of the protein actin. Researchers led by Yale E. Goldman at the University of Pennsylvania in Philadelphia attached a dye to a myosin subunit, then used superfast switching of polarized light from multiple directions to take microsecond-scale snapshots that revealed the subunit's orientation and rotations.