Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface.
Nuclear magnetic resonance (NMR) measurements provide both structural and dynamical information about the molecules in which nuclear resonances are observed. This manuscript addresses NMR relaxation of water protons in protein powder systems. Inclusion of magnetic communication between the water proton spins and protein proton spins leads to a clearer view of water molecule dynamics at the protein surface than has been previously available. We conclude that water molecule motion at the protein surface is somewhat slower than in the solute free solvent, but it is orders of magnitude faster than motions in a rigid ice lattice even in samples hydrated to levels well below what is generally thought to be the full hydration complement of the protein. The NMR relaxation data on lysozyme powders support a model that leaves adsorbed water very fluid at the protein surface with reorientational correlation times for the water shorter than nanoseconds.
D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009113:Muramidase; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D013696:Temperature; D014867:Water
D011506:Proteins; D014867:Water; D009113:Muramidase