High-Density Hydration layer of Lysozyme: Molecular Dynamics Decomposition of Solution Scattering Data

Journal Article · Sun May 01 04:00:00 EDT 2005 · Journal of Chemical Information and Modeling

OSTI ID:932189

Smith, Jeremy C ^[1]; Merzel, Franci ^[2]

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1. ORNL
2. National Institute of Chemistry, Solvenia

A characterization of the physical properties of protein hydration water is critical for understanding protein structure and function. Recent small-angle X-ray and neutron scattering data indicate that the density of water on the surface of lysozyme is significantly higher than in bulk water. Here, we provide an interpretation of the scattering results using a molecular dynamics simulation, which allows us to make quantitative predictions about density variations in the first hydration shell. The perturbation relative to bulk water involves statistically significant changes in the average water structure in the first hydration layer. The water density in the first hydration shell is increased by 5% with respect to the bulk. In regions of higher water density, the water dipoles align more parallel to each other and the number of hydrogen bonds per water molecule is higher. Increased water density is found for water molecules interacting with hydrogen and carbon atoms in the backbone or with nonpolar or negatively charged side-chain groups.

• Research Organization: Oak Ridge National Laboratory (ORNL)
• Sponsoring Organization: ORNL Program Development
• DOE Contract Number: AC05-00OR22725
• OSTI ID: 932189
• Journal Information: Journal of Chemical Information and Modeling, Journal Name: Journal of Chemical Information and Modeling Vol. 45
• Country of Publication: United States
• Language: English

Related Subjects

08 HYDROGEN
ATOMS
CARBON
DIPOLES
HYDRATION
HYDROGEN
LYSOZYME
NEUTRONS
PHYSICAL PROPERTIES
PROTEIN STRUCTURE
PROTEINS
SCATTERING
SIMULATION
WATER