Pathways and intermediates in forced unfolding of spectrin repeats.

@article{Altmann2002PathwaysAI,
  title={Pathways and intermediates in forced unfolding of spectrin repeats.},
  author={Stephan M. Altmann and Raik G Gr{\"u}nberg and Pierre-François Lenne and Jari Yl{\"a}nne and Arnt Johan Raae and Kristina M Herbert and Matti Saraste and Michael Nilges and J. K. Heinrich H{\"o}rber},
  journal={Structure},
  year={2002},
  volume={10 8},
  pages={
          1085-96
        }
}
Spectrin repeats are triple-helical coiled-coil domains found in many proteins that are regularly subjected to mechanical stress. We used atomic force microscopy technique and steered molecular dynamics simulations to study the behavior of a wild-type spectrin repeat and two mutants. The experiments indicate that spectrin repeats can form stable unfolding intermediates when subjected to external forces. In the simulations the unfolding proceeded via a variety of pathways. Stable intermediates… CONTINUE READING
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