Presented by

Dr. Ruedi Aebersold

Biological or clinical phenotypes arise from the biochemical state of a cell which, in turn, is the result of the composition and state of activity of biomolecules and their organization in the cell. Technological advances have made the systematic measurement of different biomolecules a reality: OMICS technologies. Frequently, data generated across different OMICS layers are integrated with the aim of provide complementary information on the state of the cell.

Proteins are the functionally most important biomolecules. They catalyse and control most biochemical reactions and it is generally assumed that the proteome state closely determines the biochemical state of the cell. To date, most proteomic measurements have focused on the identification and quantification of one or several polypeptides per protein coding gene. Yet the proteome contains multiple layers of additional highly relevant functional information, including the resolution of products of specific genes into multiple proteoforms via alternative splicing or PTM’s, protein conformation and structure, and the organization of proteins into complexes and interaction networks. In this presentation we will discuss mass spectrometry-based methods to systematically measure multiple layers of proteomic information. We argue that the information gained from integrating different proteomic layers is functionally highly informative and provides a unique basis to support mechanistic models of biological processes.