Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils.

@article{Minajeva2001UnfoldingOT,
  title={Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils.},
  author={Ave Minajeva and Michael Kulke and J. M. Fern{\'a}ndez and Wolfgang A Linke},
  journal={Biophysical journal},
  year={2001},
  volume={80 3},
  pages={1442-51}
}
The elastic section of the giant muscle protein titin contains many immunoglobulin-like domains, which have been shown by single-molecule mechanical studies to unfold and refold upon stretch-release. Here we asked whether the mechanical properties of Ig domains and/or other titin regions could be responsible for the viscoelasticity of nonactivated skeletal-muscle sarcomeres, particularly for stress relaxation and force hysteresis. We show that isolated psoas myofibrils respond to a stretch-hold… CONTINUE READING
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