Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: implications for protein engineering.

@article{Reiersen1998ShortEP,
  title={Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers: implications for protein engineering.},
  author={Herald Reiersen and Adam R Clarke and Anthony Robert Rees},
  journal={Journal of molecular biology},
  year={1998},
  volume={283 1},
  pages={
          255-64
        }
}
Elastin is a major protein component of the vascular wall and is responsible for its unusual elastic properties. Polymers of its repeating VPGVG sequences have been synthesised and shown to exhibit an inverse temperature transition where, as temperature rises, the polymer collapses from an extended chain to a beta-spiral structure with three VPGVG units per turn, each pentamer adopting a type II beta-turn conformation. These studies, however, have not established whether the temperature-driven… CONTINUE READING
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