Dr. Borchers is the head of the proteomics core at the University of North Carolina in Chapel Hill and holds the position of Assistant Professor at the University. His main interests lie in methodologies for quantification of proteins and use of photochemical reactions to aid in protein identification.
Mass spectrometry has been well-recognized for its ability to provide accurate mass measurements of biomolecules which allows the rapid and sensitive study of proteins from a given genome in a large-scale manner at a single experiment (proteomics). The current proteomics approaches are very powerful in identifying proteins, however, they lack the ability of absolute protein quantification, comprehensive identification as well as in identification and quantification of protein modifications (like phosphorylation) in a large-scale manner. All these features are important for a more complete characterization of the protein differences in sick versus healthy cells which provides a more complete knowledge about the disease involving proteins and protein pathways. One of our research goals is to develop and apply novel proteomics methods based on the combination of protein chemistry and mass spectrometric approaches allowing protein characterization and its modification, comprehensively and quantitatively.
Another main focus of our research is the combined approach of photochemical reactions at proteins and mass spectrometric methods. This concept is suitable for identification of target proteins and components of protein complexes, structural characterization of protein-lagan and protein-biomolecule interaction, and elucidation of dynamic processes in proteins. The photochemical reactions at proteins used for this purpose can be classified as photoaffinity labeling, photo-crosslinking, or time-resolved photochemical reactions. The purpose of the research is to develop and apply this concept in order to provide information relevant to a number of health concerns and biochemical and pharmaceutical processes. For this research, our special interest is to identify the binding partners of the tumor suppressor protein p53 at different phosphorylation states of p53 and different cell states in a time-dependant manner to elucidate the involvement of p53 in the apoptosis and cell growth pathway.