Solvent-induced backbone fluctuations and the collective librational dynamics of lysozyme studied by terahertz spectroscopy.

  • Kristina N. Woods
  • Published 2010 in
    Physical review. E, Statistical, nonlinear, and…

Abstract

THz spectroscopy is used to investigate the dynamics of the globular protein hen egg white lysozyme under varying hydration and temperature conditions. An analysis of the experimental spectra has revealed that the amount of solvent in the hydration shell has a strong influence on the low-frequency protein conformational dynamics and also the arrangement of hydrogen bonds in the protein secondary structure. Furthermore at a hydration level >0.2 we identify collective backbone fluctuations in the protein secondary structure that are not present at low hydration. It is possible that these solvent induced modes are important for the biological function of the protein.

Cite this paper

@article{Woods2010SolventinducedBF, title={Solvent-induced backbone fluctuations and the collective librational dynamics of lysozyme studied by terahertz spectroscopy.}, author={Kristina N. Woods}, journal={Physical review. E, Statistical, nonlinear, and soft matter physics}, year={2010}, volume={81 3 Pt 1}, pages={031915} }