RTG 768: Biomolecular Switches - Coding of Proteins via Conformational Changes and Posttranslational Modifications

For some species the entire set of proteins - the proteome - can be derived from the knowledge of the genomic sequences. This knowledge, however, does not provide direct access to the understanding of the complex phenotypes of living organisms. The very diverse phenotypes and tasks of organisms cannot be derived from the molecular assembly of cells in a direct manner. Therefore, a detailed analysis of the complex interactions of proteins and their relevance for the phenotypes of cells and organisms moves into the focus of current molecular biological research.In the research training group "Biomolecular Switches" the question is addressed how signaling proteins are modulated in their structure and function by means of posttranslational modifications or by conformational changes induced by other means. Thus, we are interested in how such processes contribute to a diversification of protein structure and function, not directly deducible from the genome. For selected examples, various conformational states of proteins are investigated with respect to their structure and their functional consequences. We consider proteins as Biomolecular Switches and try to contribute to the understanding of their modes of operation. Two major questions are addressed: -What is the correlation between alternative structural and functional states of such proteins?-What is the interplay between molecularly defined states of proteins and their cellular functions?Correspondingly, the research training group is organized in two project areas. These focus on "Molecular States and Mechanisms" and on "Cellular Functions", respectively.