Glycosylation represents not only one of the most common post-translational modifications of proteins but is by far the most diverse (with literally thousands of different glycans possible at a given site of modification).
In this webcast, Dr. Lance Wells of the Complex Carbohydrate Research Center, University of Georgia, will cover methods for determining sites of modification for both N- and O-linked glycosylation. He will also discuss approaches for quantitatively determining occupancy and with N-linked glycosylation expand to include N-linked type (high Mannose versus hybrid/complex). While most of the procedures for site-mapping involve the release of the glycan from the underlying polypeptide backbone, the ultimate goal is to perform direct glycopeptide analyses. Thus, in the second half of the presentation, he will focus on direct glycopeptide approaches on the Thermo Scientific - Orbitrap Fusion Lumos mass spectrometer that allow one to observe the microheterogeneity at specific sites on proteins. Methods to be covered include combinations of pseudo-neutral loss and/or oxonium ion triggered MSn events, Step-HCD, and EThcD. Software solutions are also discussed including Byonic and pGlyco 2.1.
In this webcast, you will learn the:
- Latest mass spectrometry techniques for characterizing intact glycopeptides
- Use of mass spectrometry for determining sites of modification and microheterogeneity for both N- and O-linked glycosylation
- Latest software solutions for glycoproteomics
