Principal components of the protein dynamical transition.

@article{Tournier2003PrincipalCO,
  title={Principal components of the protein dynamical transition.},
  author={Alexander L. Tournier and Jeremy C. Smith},
  journal={Physical review letters},
  year={2003},
  volume={91 20},
  pages={
          208106
        }
}
Proteins exhibit a solvent-driven dynamical transition at 180-220 K, manifested by nonlinearity in the temperature dependence of the average mean-square displacement. Here, molecular dynamics simulations of hydrated myoglobin show that the onset of the transition at approximately 180 K is characterized by the appearance of a single double-well principal component mode involving a global motion of two groups of helices. As the temperature is raised a few more quasiharmonic and multiminimum… CONTINUE READING

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