Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.

@article{Hagen2001RateOI,
  title={Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.},
  author={Stephen J. Hagen and Caleb Carswell and E M Sjolander},
  journal={Journal of molecular biology},
  year={2001},
  volume={305 5},
  pages={1161-71}
}
We have measured the effect of temperature and denaturant concentration on the rate of intrachain diffusion in an unfolded protein. After photodissociating a ligand from the heme iron of unfolded horse cytochrome c, we use transient optical absorption spectroscopy to measure the time scale of the diffusive motions that bring the heme, located at His18, into contact with its native ligand, Met80. Measuring the rate at which this 62 residue intrachain loop forms under both folding and unfolding… CONTINUE READING