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Biophys J, September 2002, p. 1578-1588, Vol. 83, No. 3
Institut Laue Langevin, B.P.156, 38042 Grenoble Cedex 9, France
This paper reports an incoherent quasielastic
neutron scattering study of the single particle, diffusive motions of
water molecules surrounding a globular protein, the hen egg-white
lysozyme. For the first time such an analysis has been done on protein
crystals. It can thus be directly related and compared with a recent
structural study of the same sample. The measurement temperature ranged
from 100 to 300 K, but focus was on the room temperature analysis. The
very good agreement between the structural and dynamical studies suggested a model for the dynamics of water in triclinic crystals of
lysozyme in the time range ~330 ps and at 300 K. Herein, the dynamics
of all water molecules is affected by the presence of the protein, and
the water molecules can be divided into two populations. The first
mainly corresponds to the first hydration shell, in which water
molecules reorient themselves fivefold to 10-fold slower than in bulk
solvent, and diffuse by jumps from hydration site to hydration site.
The long-range diffusion coefficient is five to sixfold less than for
bulk solvent. The second group corresponds to water molecules further
away from the surface of the protein, in a second incomplete hydration
layer, confined between hydrated macromolecules. Within the time scale
probed they undergo a translational diffusion with a self-diffusion
coefficient reduced ~50-fold compared with bulk solvent. As protein
crystals have a highly crowded arrangement close to the packing of
macromolecules in cells, our conclusion can be discussed with respect
to solvent behavior in intracellular media: as the mobility is highest
next to the surface, it suggests that under some crowding conditions, a
two-dimensional motion for the transport of metabolites can be dominant.
Biophys J, September 2002, p. 1578-1588, Vol. 83, No. 3
© 2002 by the Biophysical Society 0006-3495/02/09/1578/11 $2.00
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