Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering.

@article{Diehl1997WatercoupledLM,
  title={Water-coupled low-frequency modes of myoglobin and lysozyme observed by inelastic neutron scattering.},
  author={Markus Diehl and Wolfgang Doster and Winfried Petry and Helmut Schober},
  journal={Biophysical journal},
  year={1997},
  volume={73 5},
  pages={2726-32}
}
Conformational changes of proteins often involve the relative motion of rigid structural domains. Normal mode analysis and molecular dynamics simulations of small globular proteins predict delocalized vibrations with frequencies below 20 cm(-1), which may be overdamped in solution due to solvent friction. In search of these modes, we have studied deuterium-exchanged myoglobin and lysozyme using inelastic neutron scattering in the low-frequency range at full and low hydration to modify the… CONTINUE READING