Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.

@article{Cellmer2007RelaxationRF,
  title={Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.},
  author={Troy Cellmer and Eric R Henry and Jan Kubelka and James Hofrichter and William A Eaton},
  journal={Journal of the American Chemical Society},
  year={2007},
  volume={129 47},
  pages={
          14564-5
        }
}
  • Troy Cellmer, Eric R Henry, +2 authors William A Eaton
  • Published in
    Journal of the American…
    2007
  • Chemistry, Medicine
  • The connection between free-energy surfaces and chevron plots has been investigated in a laser temperature jump kinetic study of a small ultrafast folding protein, the 35-residue subdomain from the villin headpiece. Unlike all other proteins that have been studied so far, no measurable dependence of the unfolding/refolding relaxation rate on denaturant concentration was observed over a wide range of guanidinium chloride concentration. Analysis with a simple Ising-like theoretical model shows… CONTINUE READING

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