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.
Lesage
Anne
A
Laboratoire de Chimie, UMR 5532 CNRS-ENS, Ecole Normale Supérieure de Lyon, 46, allée d'Italie, 69364 Lyon, France. anne.lesage@ens-lyon.fr
Böckmann
Anja
A
D002247:Carbon Isotopes; D006860:Hydrogen Bonding; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010750:Phosphoproteins / Q000737:chemistry*; D011522:Protons; D014867:Water / Q000737:chemistry*
D002247:Carbon Isotopes; D010750:Phosphoproteins; D011522:Protons; D014867:Water