Diversity of structural behavior in vertebrate conventional myosins complexed with actin.

@article{Iwamoto2007DiversityOS,
  title={Diversity of structural behavior in vertebrate conventional myosins complexed with actin.},
  author={Hiroyuki Iwamoto and Kazuhiro Oiwa and Mih{\'a}ly Kov{\'a}cs and James R Sellers and Takuya Suzuki and Jun'ichi Wakayama and Takumi Tamura and Naoto Yagi and Tetsuro Fujisawa},
  journal={Journal of molecular biology},
  year={2007},
  volume={369 1},
  pages={249-64}
}
Low-resolution three-dimensional structures of acto-myosin subfragment-1 (S1) complexes were retrieved from X-ray fiber diffraction patterns, recorded either in the presence or absence of ADP. The S1 was obtained from various myosin-II isoforms from vertebrates, including rabbit fast-skeletal and cardiac, chicken smooth and human non-muscle IIA and IIB species, and was diffused into an array of overstretched, skinned skeletal muscle fibers. The S1 attached to the exposed actin filaments… CONTINUE READING

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