Key result
Site-directed spectroscopic probes reveal that single biochemical states produce multiple structural states, and transitions between order and dynamic disorder power the actomyosin engine.
Site-directed spectroscopic probes reveal that the actomyosin engine is powered by transitions between states of order and dynamic disorder.
Spectroscopy of myosin and actin has entered a golden age. High-resolution crystal structures of isolated actin and myosin have been used to construct detailed models for the dynamic actomyosin interactions that move muscle. Improved protein mutagenesis and expression technologies have facilitated site-directed labeling with fluorescent and spin probes. Spectroscopic instrumentation has achieved impressive advances in sensitivity and resolution. Here we highlight the contributions of site-directed spectroscopic probes to understanding the structural dynamics of myosin II and its actin complexes in solution and muscle fibers. We emphasize studies that probe directly the movements of structural elements within the myosin catalytic and light-chain domains, and changes in the dynamics of both actin and myosin due to their alternating strong and weak interactions in the ATPase cycle. A moving picture emerges in which single biochemical states produce multiple structural states, and transitions between states of order and dynamic disorder power the actomyosin engine.
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Thomas et al. (2009) conducted a review in Actomyosin structural dynamics. Site-directed spectroscopic probes was evaluated. Site-directed spectroscopic probes reveal that single biochemical states produce multiple structural states, and transitions between order and dynamic disorder power the actomyosin engine.
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