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Naumburg Kolleg

Due to its methodical progresses during the past decade, solid-state NMR spectroscopy is increasingly important in biology. The development of superconducting high-field magnets (up to ca. 20 T for wide-bore magnets) and of magic angle spinning (MAS) devices with sample spinning rates up to 30 - 50 kHz were major reasons for this development. The principle of the MAS technique is illustrated in the left figure 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).

Our group has a modern three-channel 300 MHz solid-state NMR spectrometer to its own disposal. Furthermore, we have access to a 750 MHz high-field solid-state NMR spectrometer located at the University of Leipzig.