How does CE-MS compare with LC-MS in peptide and PTM analysis?
Professor Herbert Lindner
Head of the Protein Micro-Analysis Facility, Innsbruck Medical University
Traditional LC-MS methods struggle to identify and quantify Aspartate and iso-Aspartate isomers as they have the same mass and similar fragmentation patterns which often result in false positives. 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 traditional LCMS approaches.
In this webinar you will discover how CESI-MS has been used to tackle these difficult challenges and how it compares to nano LC-MS and find out how it has been applied to real biological samples in proteomics research.
Attend this webinar to discover:
- 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.
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