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Bidirectional Ion Transfer between Quadrupole Arrays: MSn Ion/Ion Reaction Experiments on a Quadrupole/Time-of-Flight Tandem Mass Spectrometer
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Abstract
Methods for bidirectional ion transmission between distinct quadrupole arrays were developed on a quadrupole/time-of-flight tandem mass spectrometer (QqTOF) containing three quadrupoles (ion guide Q0, mass filter Q1, and collision cell Q2) and a reflectron TOF analyzer, for the purpose of implementing multistage ion/ion reaction experiments. The transfer efficiency, defined as the percentage of ions detected after two transfer steps relative to the initial ion abundance, was found to be about 60% between Q2 and Q0 (with passage through the intermediate array (Q1)) and almost 100% between Q2 and Q1. Efficient ion transfer enabled new means for executing MSn experiments on an instrument of this type by operating Q1 in rf/dc mode for performing multiple steps of precursor/product ion isolation while passing ions through Q1 or trapping ions in Q1. In the latter case, the Q1 functioned as a linear ion trap. Either collision induced dissociation (CID) or ion/ion reactions can be conducted in between each stage of mass analysis. MS3 or MS4 experiments were developed to illustrate the charge increase of peptide ions via two steps of charge inversion ion/ion reactions, CID of electron-transfer dissociation (ETD) products and CID of a metal−peptide complex formed from ion/ion reactions.
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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Electron Transfer Dissociation Facilitates the Measurement of Deuterium Incorporation into Selectively Labeled Peptides with Single Residue Resolution
Martin Zehl, Kasper D. Rand, Ole N. Jensen and Thomas J. D. JørgensenJournal of the American Chemical Society2008 130 (51), 17453-17459Electron Transfer Dissociation Facilitates the Measurement of Deuterium Incorporation into Selectively Labeled Peptides with Single Residue Resolution
Martin Zehl, Kasper D. Rand, Ole N. Jensen and Thomas J. D. JørgensenJournal of the American Chemical Society2008 130 (51), 17453-17459Mass spectrometry is routinely applied to measure the incorporation of deuterium into proteins and peptides. The exchange of labile, heteroatom-bound hydrogens is mainly used to probe the structural dynamics of proteins in solution, e.g., by hydrogen-...
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History
- Published In Issue November 01, 2007
- Received for review July 8, 2007. Accepted August 30, 2007.
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