Construction of a hybrid quadrupole/fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10 kDa

  • Steven M. Patrie
  • Jay P. Charlebois
  • David Whipple
  • Neil L. Kelleher
  • Christopher L. Hendrickson
  • John P. Quinn
  • Alan G. Marshall
  • Biswarup Mukhopadhyay
Focus: McLafferty Rearrangement

DOI: 10.1016/j.jasms.2004.04.031

Cite this article as:
Patrie, S.M., Charlebois, J.P., Whipple, D. et al. J Am Soc Mass Spectrom (2004) 15: 1099. doi:10.1016/j.jasms.2004.04.031

Abstract

Technological advancements including an open-cylindrical Penning trap with capacitively coupled ICR cell, selective ion accumulation with a resolving quadrupole, and a voltage gradient used during ion extraction from an octopole ion trap, have individually improved dynamic range and sensitivity in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry (FT-ICR MS). Documented here is a new instrument utilizing these technologies toward the robust detection and fragmentation of biomolecules >10 kDa. Up to 55-fold enhancement in ion population by selective ion accumulation combined with 10- to 20- fold signal-to-noise improvement by application of a DC voltage gradient to an accumulation octopole during the ion transfer event offers improved signal-to-noise (or speed) of MS/MS experiments, for proteins from Methanococcus jannaschii and Saccharomyces cerevisiae whole cell lysates. After external quadrupole filtering with a 40 m/z window, three proteins were fragmented (and identified) in parallel from the database of Methanococcus jannaschii. Electron capture dissociation (ECD) of an intact yeast protein provides extensive sequence information resulting in a high degree of localization for an N-terminal acetylation. Hybrid fragmentation, infrared multiphoton dissociation (IRMPD) followed by low energy electrons (ECD), with the electron source located laterally off the z-axis and external to the magnet bore, presents a strategy for identification of proteins by means of the sequence tag approach. Automated implementation of diverse MSn approaches in a Q-FTMS instrument promises to help realize “top-down” proteomics in the future.

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Copyright information

© American Society for Mass Spectrometry 2004

Authors and Affiliations

  • Steven M. Patrie
    • 1
  • Jay P. Charlebois
    • 1
  • David Whipple
    • 1
  • Neil L. Kelleher
    • 1
  • Christopher L. Hendrickson
    • 2
  • John P. Quinn
    • 2
  • Alan G. Marshall
    • 2
    • 3
  • Biswarup Mukhopadhyay
    • 4
  1. 1.Department of Analytical ChemistryUniversity of IllinoisUrbanaUSA
  2. 2.Ion Cyclotron Resonance Program, National High Magnetic Field LaboratoryFlorida State UniversityTallahasseeUSA
  3. 3.Department of Chemistry and BiochemistryFlorida State UniversityTallahassee
  4. 4.Departments of Biochemistry and BiologyVirginia Bioinformatics Institute, Virginia TechBlacksburgUSA