Abstract
The mean square displacements (MSD) of a model protein, the maltose binding protein, and its hydration water have been estimated from the elastic neutron scattering intensity measured on the IN5 time-of-flight spectrometer. The availability of the protein in both fully deuterated and hydrogenated form allowed reliable separation of the contribution of the solvent interacting with the biomolecule from that of the hydrated biomolecule. The thermal fluctuations of hydration water and protein activate in the same temperature range between 200–220 K. This result supports a picture where the dynamical coupling between the biomolecule and the solvent is already effective in the picosecond timescale. A quantitative agreement of the MSD, with values from molecular dynamics simulations, is found.
Acknowledgements
The Institute Laue-Langevin (ILL) is kindly acknowledged for providing beam time and technical and scientific support. The authors are grateful to Dr. J. Ollivier for assistance during the experiment on the IN5 spectrometer. This work has benefited from the activities of the DLAB consortium, funded by the EU under contracts HPRI-2001-50065 and RII3-CT-2003-505925, and from UK EPSRC-funded activity within the ILL-EMBL Deuteration Laboratory under grants GR/R99393/01 and EP/C015452/1.