Water−Protein Interactions in Microcrystalline Crh Measured by ¹H−¹³C Solid-State NMR Spectroscopy

Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural features of the protein such as hydrogen-bonding or salt-bridge networks.