Deuterated Peptides and Proteins: Structure and Dynamics Studies by MAS Solid-state NMR

The use of perdeuterated proteins yields a significant improvement in the resolution and the sensitivity of MAS solid-state NMR experiments. In particular, the amide protons in the protein backbone become available for correlation spectroscopy. Specific labeling schemes allow the detection of high resolution methyl proton spectra. Dilution of the proton spin system enables a spin-diffusion-free determination of dynamic parameters such as 15N-T 1 and 15N-CSA and 1H–15N dipole cross-correlated relaxation that yields T 2-type information in the solid state. Side-chain dynamic information is accessible by making use of the deuterium quadrupolar interaction by the interpretation of the spinning sideband manifold.