Agilent Technologies: Electron Fragmentation for the Agilent Q-TOF Family
In collaboration with e-MSion, we have an option for electron fragmentation of peptides and proteins with the Agilent 6500 Series Quadrupole Time-of-Flight LC/MS (Q-TOF) systems. LC-MS/MS for proteomics typically involves collision-induced dissociation (CID) of the precursor peptide ions to produce sequence-specific fragment ions.
CID occurs by the lowest energy pathways generating backbone b and y ions where labile post-translational modifications (PTMs) are often lost. ECD results from the irradiation of ions with low-energy electrons where the N–Cα backbone bond is cleaved producing c and z ions. With ECD, labile PTMs are retained on peptide backbone fragments enabling site localization of modifications.
Presenter: Rebecca Glaskin, PhD (LC/MS Application Scientist, Agilent Technologies, Inc.)
Rebecca Glaskin is an LC/MS Application Scientist at Agilent with a focus on BioPharma applications supporting the LC-Q/TOF and IM-QTOF platforms. Prior to joining Agilent, Rebecca received her Ph.D. in analytical chemistry from Indiana University in the lab of Professor David Clemmer. While there she designed and constructed home-built instruments, pushing the limits of the mobility resolution that can be obtained with a circular drift tube for the separation of biomolecules (peptides, proteins, carbohydrates, and metabolites). While there, she also studied hydrogen/deuterium exchange of proteins in the gas-phase as a function of time and pressure. Rebecca then went to Boston University as a Postdoctoral Associate in the lab of Professor Catherine Costello to develop a database containing collision cross section values for glycans, peptides, and glycopeptides utilizing Agilent Technologies 6560 IM-QTOF. This database can be used to determine how the collision cross section is altered with the addition of individual saccharide units. The trendlines obtained from this database will be used to predict collision cross sections for glycopeptides based on the conformation and structure of the specific glycoform.