High-density hydration layer of lysozymes: Molecular dynamics decomposition of solution scattering data

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 oil the surface of lysozyme is significantly higher than in bulk water. Here, we provide all interpretation of the scattering results using a molecular dynamics simulation, which allows Lis 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 ill the backbone or with nonpolar or negatively charged side-chain groups.