Solvent-induced backbone fluctuations and the collective librational dynamics of lysozyme studied by terahertz spectroscopy.
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.
Woods
K N
KN
Physics Department, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. knwoods@cmu.edu
D003198:Computer Simulation; D004795:Enzyme Stability; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D055068:Terahertz Spectroscopy / Q000379:methods*
D012997:Solvents; D009113:Muramidase