Prof. Dr. Raphael Stoll

AG Biomolekulare NMR
Faculty of Chemistry and Biochemistry

Research program

A detailed understanding of the function of a biological macromolecule requires knowledge of its three-dimensional structure. With the completion of the human genome project, an even greater challenges awaits the biologists: structural genomics and proteomics, the study of all proteins coded by the genes of an organism. Obviously, proteins are now the focus in life science, as they trigger many biochemical pathways and are often the key to diseases.

Efficient techniques for incorporation of stable NMR active 13 C and 15 N isotopes into recombinant proteins expressed in E. coli have resulted in dramatic advances in the design and implementation of multidimensional NMR spectroscopic methods. Concomitant developments of modern molecular biology and multidimensional NMR spectroscopy have increased explosively by the use of NMR for generating structural and dynamical information on biological molecules. The maturation of the field of structural biology has now made the study of structure-function relationships of biological macromolecules by NMR spectroscopy an integral part of diverse biochemical research efforts. NMR spectroscopy does not only provide structural data but reaches much further and can provide information on dynamics, conformational equlibria, folding, and intra- as well as intermolecular interactions.

We mainly focus on nuclear magnetic resonance (NMR) spectroscopy to elucidate the structure in solution of key proteins of the nervous system, such as PDZ protein-protein interaction domains or small GTPases of the Ras superfamily. In addition, we use molecular biological and biochemical techniques in close collaboration with Prof. Dr. Heumann's group to clone, express, purify, and characterize the functional behaviour of these proteins.