Post translational modifications (PTMs) are important indicators of change in cells. Two of the top four most abundant PTMs are deamidation and phosphorylation. LC-MS methods struggle to identify and quantify Aspartate and iso-Aspartate isomers (associated with deamidation) as they have the same mass and similar fragmentation patterns which often result in false positives. Location of the phosphorylation site is important in understanding the effect of this modification on the activity of proteins. Phosphorylated peptides are often polar and elute early in traditional LC analyses and positional isomers of phosphorylated peptides are identical in mass and have very similar fragmentation patterns which makes their identification difficult by LC-MS.
Join Professor Herbert Linder, Head of the Protein Micro-Analysis Facility at Innsbruck Medical University, as he shares with you how CESI-MS has been used to tackle these challenges and how it compares to LC-MS and find out how it has been applied to real biological samples in proteomics research.
After listening to this on-demand webinar, you will understand:
- Why CESI-MS is ideal for separating and detecting phosphopeptide isomers
- How CESI-MS can detect additional PTMs missed by nano LC-MS
- How CESI-MS can be used in the study of biological extracts, e.g. the detection of modification sites in H1 Histones
- How CESI-MS can be used to detect a Peptide that has been associated with fungal infections and how this approach differs from an LC-MS approach
You should attend this webinar if you are:
- Scientists in academia, government and the pharmaceutical industry involved in proteomics research and peptide analysis
- R&D and analytical development directors, laboratory managers and scientists at biopharmaceutical companies and contract research labs interested in PTM mapping
- Academics working in proteomics research