Research Group Functional Proteome Analysis

Proteomes change qualitatively and quantitatively, reflecting the alterations in the physiological state of cells, body fluids, organelles and organisms. This is not only achieved by the expression of different genes and proteins, but also by a large number of posttranslational events giving rise to the high complexity on the protein level. In recent years, mass spectrometry has emerged to be one of the most powerful tools to study proteomes, protein networks and multiprotein platforms. In collaborative projects with clinical partners our research group “Functional Proteome Analysis” is participating in several long-term research activities including mainly three areas: (I) large scale investigation of so far unknown proteomes, (II) quantitative description of posttranslational modifications, and (III) relative and absolute quantification of proteins and protein complexes. To this end we are applying metabolic labeling with heavy isotopes as well as label-free approaches to obtain comprehensive information to uncover the dynamics and interactions of protein networks.

FUTURE OUTLOOK
Applying mass spectrometry to investigate and quantitatively describe protein interactions and networks.