Solid-State NMR spectroscopy
Due to its methodical progresses during the past decades, solid-state NMR spectroscopy is increasingly important in biology. The development of superconducting high-field magnets (up to ca. 25 T for wide-bore magnets) and of magic angle spinning (MAS) devices with maximum sample spinning rates beyond 100 kHz were major reasons for this development. The principle of the MAS technique is illustrated in the figures together with a highly resolved P-31 {H-1} cross-polarisation MAS NMR spectrum of a nucleotide (GppCH2p) bound to a protein (Ras). The sample under study was a microcrystalline protein put into the 2.5 mm-MAS rotor together with its mother liquor (see Iuga et al., J. Mol. Biol. 342 (2004) 1033).
Resolution and sensitivity achived in recent solid-state NMR experiments of proteins are sufficient to apply multidimensional NMR techniques similar to the experiments applied in liquid-state biomolecular NMR spectroscopy.
The right figure shows a two-dimensional H-1-driven P-31-P-31 spin diffusion spectrum of a nucleotide (GppCH2p) bound to a protein (Ras).
13C MAS NMR Spectroscopy is, for example, an excellent tool for the characterization of Metal-Organic Frameworks as well as the dynamic behavior of several structural groups.
Our group has two modern three-channel 800 MHz and 300 MHz solid-state NMR spectrometer to its own disposal.