Selected fragment scans of mass spectrometers in direct mixture analysis

Zakett, D.; Schoen, Alan; Kondrat, R. W.; Cooks, R. Graham

doi:10.1021/ja00516a064

Cited by 42 publications

(23 citation statements)

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“…First experimented in the late 1970s in order to screen particular functional groups in complex mixtures [12], the CNLS-MS/MS technique remains rarely used. Neutral loss experiments consist of monitoring the loss of a neutral fragment produced by the fragmentation of a precursor ion in a collision cell.…”

Section: Introductionmentioning

confidence: 99%

Carboxylic acid functional group analysis using constant neutral loss scanning-mass spectrometry

Dron¹,

Eyglunent²,

Temime-Roussel³

et al. 2007

Analytica Chimica Acta

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Section: Introductionmentioning

confidence: 99%

Carboxylic acid functional group analysis using constant neutral loss scanning-mass spectrometry

Dron¹,

Eyglunent²,

Temime-Roussel³

et al. 2007

Analytica Chimica Acta

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“…MS/MS as an analytical technique was still in its infancy, with the research groups of Cooks and McLafferty at the forefront of the development [1][2][3][4][5][6][7][8][9][10][11][12]. For all this early work, sector instruments were used exclusively and CID was performed at high kinetic energies.…”

Section: Beam-beam Hybrid Instrumentsmentioning

confidence: 99%

Hybrid mass spectrometers for tandem mass spectrometry

Glish

Burinsky

2008

J. Am. Soc. Mass Spectrom.

103

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Mass spectrometers that use different types of analyzers for the first and second stages of mass analysis in tandem mass spectrometry (MS/MS) experiments are often referred to as "hybrid" mass spectrometers. The general goal in the design of a hybrid instrument is to combine different performance characteristics offered by various types of analyzers into one mass spectrometer. These performance characteristics may include mass resolving power, the ion kinetic energy for collision-induced dissociation, and speed of analysis. This paper provides a review of the development of hybrid instruments over the last 30 years for analytical applications. (J Am Soc Mass Spectrom 2008, 19, 161-172) © 2008 American Society for Mass Spectrometry T andem mass spectrometry (MS/MS), in a very generic description, is a process in which an ion formed in an ion source is mass-selected in the first stage of analysis, reacted, and then the charged products from the reaction are analyzed in the second stage of analysis. The type and quality of data that is obtained can vary greatly depending upon the type of analyzer used in the first and second stages of analysis, and the type of reaction performed between the stages of analysis. The reactions that can be done also can depend upon the type of analyzer. Over the years there have been a variety of means developed to measure the mass-to-charge ratio of gas-phase ions. The most common methods involve: dispersion based on ion momentum or kinetic energy (magnetic and electric sector instruments); separation in time based on ion velocity (time-of-flight); transmission through an electrodynamic field (quadrupole mass filter); and periodic motion in a magnetic or electrodynamic field (ion traps). There are differences in the experimental parameters associated with these various analysis methods that are pertinent to the MS/MS experiment. Some parameters are obvious, typically related to the performance of the mass analyzer while others are more subtle, related to the reactions/chemistry occurring between the stages of analysis. Many times these different parameters are used to categorize MS/MS experiments.One parameter is the ion kinetic energy. Sector and time-of-flight (TOF) instruments typically operate at "high" ion kinetic energies (5-20 keV), whereas "low" ion kinetic energies (Ͻ50 eV) are typical in quadrupole mass filters and ion traps. The ion kinetic energy is an important parameter in MS/MS experiments because the most common reaction involves colliding the ion of interest with a target gas atom or molecule. When performing ion-neutral collision experiments, the possible reactions that can be accessed (e.g., collisioninduced dissociation, collisional cooling, charge permutation, ion/molecule reaction) depends upon the ion kinetic energy. The appearance of the MS/MS spectrum can change drastically as a function of the collision (ion kinetic) energy. A related factor that is equally important, but often not considered, is the time frame of the experiment, that is, the elapsed time bet...

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“…Currently available instruments [17][18][19][20][21][22][23][24][25][26] are very inefficient for such linked-scan analyses (Fig. 1A).…”

Section: Theorymentioning

confidence: 99%

“…Currently, the only technique that approximates such an analysis is the linked-scan mode available in triple quadrupole, quadrupole-quadrupole time-of-flight, ion trap, and sector instruments [17][18][19][20][21][22][23][24][25][26]32]. However, instead of producing complete MS/MS fragmentation spectra of every species in the m/z range of the instrument, the technique produces only spectra of those precursor ions that generate a particular ion product or a particular neutral loss.…”

Section: Introductionmentioning

confidence: 99%

A novel high-capacity ion trap-quadrupole tandem mass spectrometer

Krutchinsky¹,

Cohen

Chait

2007

International Journal of Mass Spectrometry

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We describe a prototype tandem mass spectrometer that is designed to increase the efficiency of linked-scan analyses by >100-fold over conventional linked-scan instruments. The key element of the mass spectrometer is a novel high ion capacity ion trap, combined in tandem configuration with a quadrupole collision cell and a quadrupole mass analyzer (i.e. a TrapqQ configuration). This ion trap can store >10 6 ions without significant degradation of its performance. The current mass resolution of the trap is 100-450 full width at half maximum for ions in the range 800-4000 m/z, yielding a 10-20 m/z selection window for ions ejected at any given time into the collision cell. The sensitivity of the mass spectrometer for detecting peptides is in the low femtomole range. We can envisage relatively straightforward modifications to the instrument that should improve both its resolution and sensitivity. We tested the tandem mass spectrometer for collecting precursor ion spectra of all the ions stored in the trap and demonstrated that we can selectively detect a phosphopeptide in a mixture of non-phosphorylated peptides. Based on this prototype instrument, we plan to construct a fully functional model of the mass spectrometer for detecting modification sites on proteins and profiling their abundances with high speed and sensitivity.

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Selected fragment scans of mass spectrometers in direct mixture analysis

Cited by 42 publications

References 0 publications

Carboxylic acid functional group analysis using constant neutral loss scanning-mass spectrometry

Carboxylic acid functional group analysis using constant neutral loss scanning-mass spectrometry

Hybrid mass spectrometers for tandem mass spectrometry

A novel high-capacity ion trap-quadrupole tandem mass spectrometer

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