All processes of life are basically due to the action of proteins. Thus, there is a general interest in protein structure, function, dynamics and in the principles and mechanisms which lead to the formation of the functional state. Detailed information about spatil structures of protein has so far been obtained mainly from diffraction studies with single crystals. Thus, there is an important need to have methods available which can determine the solution structures of proteins with resolution comparable to X-ray crystallography. NMR is a unique tool for such investigations. It provides a manifold of signals which can be used to determine protein structures with high spatial resolution. In addition, the NMR data can be used to localize and characterize internal motions. With the concept of sequential resonance assignments, obtaining complete assignments of NMR spectra has become routine work for samll proteins. This now allows us to characterize in detail structural and dynamic aspects of proteins in non-crystalline environments. The strategies for such analyses are only developed in part. They are at an early state and far from being optimized. Dr. Wagner will improve these strategies for structure analysis and utilize them for studies of protein structure and function.
