The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.

@article{Hilbert2013TheKO,
  title={The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.},
  author={Lennart Hilbert and Shivaram Cumarasamy and Nedjma B. Zitouni and Michael C. Mackey and Anne-Marie Lauzon},
  journal={Biophysical journal},
  year={2013},
  volume={105 6},
  pages={1466-74}
}
Naturally occurring groups of muscle myosin behave differently from individual myosins or small groups commonly assayed in vitro. Here, we investigate the emergence of myosin group behavior with increasing myosin group size. Assuming the number of myosin binding sites (N) is proportional to actin length (L) (N = L/35.5 nm), we resolve in vitro motility of actin propelled by skeletal muscle myosin for L = 0.2-3 μm. Three distinct regimes were found: L < 0.3 μm, sliding arrest; 0.3 μm ≤ L ≤ 1 μm… CONTINUE READING
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