Nuclear magnetic resonance (NMR) has become an important technique for the determination of the three-dimensional structure of biological macromolecules. The ability to characterize both solution structure and dynamics, possibly in the presence of physiological partners, have made NMR an essential tool for understanding biological processes. The study of molecular complexes, even in the case of weak affinity, opens up powerful opportunities for the development of pharmacologically active molecules. NMR spectroscopy provides access to a wide range of biomolecular systems in solution, in cell extracts or living cells, in lipid micelles, in a micro-crystalline environment, or in a biological membrane.
Access to 950, 850, 700, and several 600 MHz instruments, equiped with most recent Bruker electronics (Avance III HD) and cryogenically cooled probes for high-sensitivity solution-state NMR applications. Standard Bruker experiment libraries, as well as additional in-house libraries for optimized fast NMR data acquisition (e.g. SOFAST, BEST, and HADAMAC-type experiments) are available. Fast-mixing equipments required for real-time studies of kinetic processes such as protein folding are also available.
Access to 950 and several 600 MHz instruments, equiped with state-of-the-art magic-angle spinning (MAS) capabilities, and triple-resonance probes for different rotor sizes and spinnning speeds.
Special accesory: Automatic sample changer for up to 24 NMR tubes