Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.

@article{Littlefield2008SimilaritiesAD,
  title={Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.},
  author={K. Littlefield and A. Ward and J. S. Chappie and M. Reedy and S. Bernstein and R. Milligan},
  journal={Journal of molecular biology},
  year={2008},
  volume={381 3},
  pages={
          519-28
        }
}
The structure and function of myosin crossbridges in asynchronous insect flight muscle (IFM) have been elucidated in situ using multiple approaches. These include generating "atomic" models of myosin in multiple contractile states by rebuilding the crystal structure of chicken subfragment 1 (S1) to fit IFM crossbridges in lower-resolution electron microscopy tomograms and by "mapping" the functional effects of genetically substituted, isoform-specific domains, including the converter domain, in… Expand

References

SHOWING 1-10 OF 41 REFERENCES
The converter domain modulates kinetic properties of Drosophila myosin.
Electron tomography of swollen rigor fibers of insect flight muscle reveals a short and variably angled S2 domain.
Myosin isoforms show unique conformations in the actin-bound state
Visualizing myosin's power stroke in muscle contraction.
  • M. Reedy
  • Chemistry, Medicine
  • Journal of cell science
  • 2000
Formation of reverse rigor chevrons by myosin heads
The structure of the rigor complex and its implications for the power stroke.
...
1
2
3
4
5
...