Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions.

@article{Fenimore2004BulksolventAH,
  title={Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions.},
  author={Paul W. Fenimore and Hans Frauenfelder and Benjamin H. McMahon and Robert D. Young},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 40},
  pages={14408-13}
}
The concept that proteins exist in numerous different conformations or conformational substates, described by an energy landscape, is now accepted, but the dynamics is incompletely explored. We have previously shown that large-scale protein motions, such as the exit of a ligand from the protein interior, follow the dielectric fluctuations in the bulk solvent. Here, we demonstrate, by using mean-square displacements (msd) from Mossbauer and neutron-scattering experiments, that fluctuations in… CONTINUE READING

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