title: Activation of intact electron-transfer products of polypeptides and proteins in cation transmission mode ion/ion reactions.
abstract: Cationic peptide electron-transfer products that do not fragment spontaneously are exposed to ion trap collisional activation immediately upon formation while they pass through a high-pressure collision cell (Q2), where the electron-transfer reagent anions are stored. Radial ion acceleration, which is normal to the ion flow, is implemented by applying an auxiliary dipolar alternating current to a pair of opposing rods of the Q2 quadrupole array at a frequency in resonance with the surviving electron-transfer products. Collisional cooling of cations in the pressurized Q2 ensures efficient overlap of the positive and negative ions for ion/ion reactions and also gives rise to relatively long residence times (milliseconds) for ions in Q2, making it possible to fragment ions via radial excitation during their axial transmission. The radial activation for transmission mode electron-transfer ion/ion reactions has been demonstrated with a doubly protonated tryptic peptide, a triply protonated phosphopeptide, and [M + 7H]7+ ions of ubiquitin. In all cases, significant increases in fragment ion yields and structural information from electron-transfer dissociation (ETD) were observed, suggesting the utility of this method for improving transmission mode ETD performance for relatively low charge states of peptides and proteins.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN 47807-2084, USA.
authors.forename: Yu
authors.initials: Y
authors.lastname: Xia
authors.forename: Hongling
authors.initials: H
authors.lastname: Han
authors.forename: Scott A
authors.initials: SA
authors.lastname: McLuckey
mesh_terms: D000595:Amino Acid Sequence; D002412:Cations / Q000737:chemistry*; D004579:Electron Transport; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis* / Q000737:chemistry*; D010748:Phosphopeptides / Q000032:analysis / Q000737:chemistry; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D011522:Protons; D025801:Ubiquitin / Q000032:analysis / Q000737:chemistry
chemical_list: D002412:Cations; D010455:Peptides; D010748:Phosphopeptides; D011506:Proteins; D011522:Protons; D025801:Ubiquitin