Design and construction of a quadruple-resonance MAS NMR probe for investigation of extensively deuterated biomolecules.

Extensive deuteration is frequently used in solid-state NMR studies of biomolecules because it dramatically reduces both homonuclear (H-H) and heteronuclear (H-C and H-N) dipolar interactions. This approach greatly improves resolution, enables low-power rf decoupling, and facilitates H-detected experiments even in rigid solids at moderate MAS rates. However, the resolution enhancement is obtained at some cost due the reduced abundance of protons available for polarization transfer.

Spatial reorientation experiments for NMR of solids and partially oriented liquids.

Motional reorientation experiments are extensions of Magic Angle Spinning (MAS) where the rotor axis is changed in order to average out, reintroduce, or scale anisotropic interactions (e.g. dipolar couplings, quadrupolar interactions or chemical shift anisotropies).