While NMR has long been used in protein-structure identification and dynamics, it is also applied now for protein-ligand binding studies. Cryogenic probes have helped to improve the sensitivity and throughput in this field, but also more and more automation is used. The hardware used in such an automatic process is shown. While the procedures mentioned are not real proteomics applications, the way to use NMR in proteomics seems to open with the development of microprobes with high sensitivity, even if the full structure is not accessable, at least a protein structure class identification should be possible. To achieve this, NMR should be coupled to Capillary electrophoresis or Capillary-Electrochromatography and even 2-dimensional chromatography. This is clearly not reached, but first steps are demonstrated to this final goal.

Metabonomics, dealing with the entity of all small molecules in biofluids or cell extracts is well established for NMR. The first application used routinely now is drug toxicity screening.

The hardware and software needed to achieve this is demonstrated as well as some examples.

In clinical research, NMR-based Metabonomics is also on the way to be a standard technology.  In the field of MEtabonomics, there is also a strong drive towards combined use of NMR and mass spectroscopy, as both technologies produce complementary results. NMR is strong on small molecules and quantification, MS is strong in sensitivity and large molecules. A system is described, combining sample preparation, measurement of NMR and LC-MS as well as common statistical data evaluation like the NMR/LC-MS covariance matrix.