NMR studies of the hydration of biological macromolecules

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Abstract
The information on the hydration of proteins and nucleic acids in aqueous solution that can be obtained using high resolution nuclear magnetic resonance (NMR) spectroscopy is largely complementary to the information obtained by diffraction experiments with single crystals, which is the only other approach enabling studies of hydration at atomic resolution. The presently discussed NMR studies are primarily focused on the rate processes governing the exchange of water molecules between the bulk solvent and the hydration sites on the biological macromolecules. A novel NMR experiment for observation of protein and nucleic acid hydration is described, and long-time molecular dynamics (MD) simulations used to support the analysis of NMR data on hydration water in the intermolecular interface of protein–DNA complexes are presented.

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