Fourier transform ion cyclotron resonance mass spectrometry: A primer

Marshall, Alan G.; Hendrickson, Christopher L.; Jackson, George S.

doi:10.1002/(sici)1098-2787(1998)17:1<1::aid-mas1>3.0.co;2-k

Cited by 1,851 publications

(1,580 citation statements)

References 131 publications

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“…In the field of complex mixture analysis, a number of methods are available to the enterprising chemist; however, Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) reigns supreme as the ‘gold standard’ technique 8, 9. Likewise, there exist a number of well‐studied complex mixtures, including natural organic matter (NOM), i.e.…”

Section: Figurementioning

confidence: 99%

Interactive van Krevelen diagrams – Advanced visualisation of mass spectrometry data of complex mixtures

Kew

Blackburn

Clarke

et al. 2017

Rapid Comm Mass Spectrometry

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Section: Figurementioning

confidence: 99%

Interactive van Krevelen diagrams – Advanced visualisation of mass spectrometry data of complex mixtures

Kew

Blackburn

Clarke

et al. 2017

Rapid Comm Mass Spectrometry

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“…Paul [1,2] and Penning [3,4] traps is a popular and powerful technique for mass analysis of polar analytes of limited or zero volatility (e.g., peptides, proteins, nucleotides, phospholipids, oligosaccharides, environmental mixtures, etc.). However, electrospray is a temporally continuous ion source, whereas mass analysis in an ion trap (Paul or Penning) is an inherently pulsed process, thereby limiting the experimental sensitivity and duty cycle.…”

Section: T He Interface Of Electrospray Ionization (Esi) Withmentioning

confidence: 99%

Improved ion extraction from a linear octopole ion trap: SIMION analysis and experimental demonstration

Wilcox

Hendrickson

Marshall

2002

J. Am. Soc. Mass Spectrom.

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Externally generated ions are accumulated in a linear octopole ion trap before injection into our 9.4 T Fourier transform ion cyclotron resonance (FT-ICR) mass analyzer. Such instrumental configuration has previously been shown to provide improved sensitivity, scan rate, and duty cycle relative to accumulated trapping in the ICR cell. However, inefficient ion ejection from the octopole currently limits both detection limit and scan rate. SIMION 7.0 analysis predicts that a dc axial electric field inside the linear octopole ion trap expedites and synchronizes the efficient extraction of the octopole-accumulated ions. Further SIMION analysis optimizes the ion ejection properties of each of three electrode configurations designed to produce a near-linear axial potential gradient. More efficient extraction and transfer of accumulated ions spanning a wide m/z range promises to reduce detection limit and increase front-end sampling rate (e.g., to increase front-end resolution for separation techniques coupled with FT-ICR mass analysis). Addition of the axial field improves experimental signal-to-noise ratio by more than an order of magnitude. (J Am Soc Mass Spectrom 2002, 13, 1304 -1312

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“…By using MALDI-FTICR (Fourier transform ion cyclotron resonance) MS it is possible to combine high resolving power, high mass accuracy, and the possibility of performing multistage MS/MS experiments [35][36][37][38] allows peptide identification directly from tissue [39].°The°FTICR°imaging°strategy°extends°the°identifi-cation possibilities in direct tissue analysis and is a valuable tool in MS imaging instrumentation.…”

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Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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Analytical methods are pursued to measure the identity and location of biomolecules down to the subcellular ( m) level. Available mass spectrometric imaging methods either compromise localization accuracy or identification accuracy in their analysis of surface biomolecules. In this study, imaging FTICR-MS is applied for the spatially resolved mass analysis of rat brain tissue with the aim to optimize protein identification by the high mass accuracy and online MS/MS capabilities of the technique. Mass accuracies up to 6 ppm were obtained in the direct MALDI-analysis of the tissue together with a spatial resolution of 200 m. The spatial distributions of biomolecules differing in mass by less than 0.1 Da could be resolved, and are shown to differ significantly. Online MS/MS analysis of selected ions was demonstrated. A comparison of the FTICR-MS imaging results with stigmatic TOF imaging on the same sample is presented. To reduce the extended measuring times involved, it is recommended to restrict the FTICR-MS analyses to areas of interest as can be preselected by other, faster imaging methods. (J Am Soc Mass Spectrom 2007, 18, 145-151)

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Fourier transform ion cyclotron resonance mass spectrometry: A primer

Cited by 1,851 publications

References 131 publications

Interactive van Krevelen diagrams – Advanced visualisation of mass spectrometry data of complex mixtures

Interactive van Krevelen diagrams – Advanced visualisation of mass spectrometry data of complex mixtures

Improved ion extraction from a linear octopole ion trap: SIMION analysis and experimental demonstration

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

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