In this session the principles behind the analysis of a number of key post-translational modifications (PTMs) using LC-MS/MS techniques will be explained. This will begin with a brief overview of bottom-up proteomics, explaining how proteins are converted to peptides, which are then analyzed using electrospray LC-MS/MS. We will move on to talk about the various MS scanning techniques, which may be used for PTM analysis. Next, we will discuss in turn, how phosphorylation, acetylation, ubiquitination, and SUMOylation may be analyzed using mass spectrometry, drawing upon real research examples. Finally, we will give opinions on the future of PTM analysis.

Topics include:

• What is proteomics and why are post-translational modifications important?
• How are proteins identified using LC-MS/MS?
• Utilizing different MS scanning functions to enable PTM detection
• How to detect both global and targeted phosphorylation events
• Approaches to acetylation studies
• How non-classical tryptic proteolysis of SUMOylated proteins enables their facile detection
• Novel approaches for ubiquitination and SUMO determination
• The future – combinatorial PTM detection with quantification?