TY - JOUR
T1 - Construction of a hybrid quadrupole/fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10 kDa
AU - Patrie, Steven M.
AU - Charlebois, Jay P.
AU - Whipple, David
AU - Kelleher, Neil L.
AU - Hendrickson, Christopher L.
AU - Quinn, John P.
AU - Marshall, Alan G.
AU - Mukhopadhyay, Biswarup
N1 - Funding Information:
The authors thank colleagues in the Kelleher Group, Greg Blakney, and Daniel McIntosh for their help and support. Funding for this project, through the laboratory of Dr. Neil Kelleher, was provided by the NSF (Career Award CHE 0134953), NIH (GM 067193), Searle Foundation, Burroughs Wellcome Fund, and the Research Corporation (Research Innovation Award). Further support was obtained from the NSF National High-Field FT-ICR Mass Spectrometry Facility (CHE 99-09502), Florida State University, and the National High Magnetic Field Laboratory at Tallahassee, Florida.
PY - 2004/7
Y1 - 2004/7
N2 - 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 MS n approaches in a Q-FTMS instrument promises to help realize "top-down" proteomics in the future.
AB - 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 MS n approaches in a Q-FTMS instrument promises to help realize "top-down" proteomics in the future.
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U2 - 10.1016/j.jasms.2004.04.031
DO - 10.1016/j.jasms.2004.04.031
M3 - Article
C2 - 15234368
AN - SCOPUS:3242717090
SN - 1044-0305
VL - 15
SP - 1099
EP - 1108
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 7
ER -