A proteomics grade electron transfer dissociation-enabled hybrid linear ion trap-orbitrap mass spectrometer.

A proteomics grade electron transfer dissociation-enabled hybrid linear ion trap-orbitrap mass spectrometer.
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DOI:
10.1021/pr800264t
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发表时间:
2008-08
影响因子:
4.4
通讯作者:
Coon, Joshua J.
Coon, Joshua J.
中科院分区:
生物学2区
文献类型:
--
作者:
McAlister, Graeme C.;Berggren, W. Travis;Griep-Raming, Jens;Horning, Stevan;Makarov, Alexander;Phanstiel, Doug;Stafford, George;Swaney, Danielle L.;Syka, John E. P.;Zabrouskov, Vlad;Coon, Joshua J.

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Here we describe the modification of a quadrupole linear ion trap-orbitrap hybrid (QLT-orbitrap) mass spectrometer to accommodate a negative chemical ionization (NCI) source. The NCI source is used to produce fluoranthene radical anions for imparting electron transfer dissociation (ETD). The anion beam is stable, robust, and intense so that a sufficient amount of reagents can be injected into the QLT in only 4 - 8 ms. Following ion/ion reaction in the QLT, ETD product ions are mass-to-charge (m/z) analyzed in either the QLT (for speed and sensitivity) or the orbitrap (for mass resolution and accuracy). Here we describe the physical layout of this device, parametric optimization of anion transport, an evaluation of relevant ETD figures of merit, and the application of this instrument to protein sequence analysis. Described proteomic applications include complex peptide mixture analysis, post-translational modification (PTM) site identification, isotope-encoded quantitation, large peptide characterization, and intact protein analysis. From these experiments we conclude the ETD-enabled orbitrap will provide the proteomic field with several new opportunities and represents an advance in protein sequence analysis technologies.
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