Force spectroscopy reveals multiple "closed states" of the muscle thin filament.

@article{Rao2011ForceSR,
  title={Force spectroscopy reveals multiple "closed states" of the muscle thin filament.},
  author={V Sreenivasa Rao and Amy Michelle Clobes and William Harold Guilford},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 27},
  pages={24135-41}
}
Tropomyosin (Tm) plays a critical role in regulating the contraction of striated muscle. The three-state model of activation posits that Tm exists in three positions on the thin filament: "blocked" in the absence of calcium when myosin cannot bind, "closed" when calcium binds troponin and Tm partially covers the myosin binding site, and "open" after myosin binding forces Tm completely off neighboring sites. However, we recently showed that actin filaments decorated with phosphorylated Tm are… CONTINUE READING