Identification and Mobility of Ions in a Townsend Discharge by Time-resolved Mass Spectrometry

McAfee, K. B.; Edelson, D.

doi:10.1088/0370-1328/81/2/125

Cited by 79 publications

(32 citation statements)

References 9 publications

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“…Although IM was first combined with mass spectrometry ( MS ) in the 1960s [2, 3], the additions of soft ionization and nested time-of-flight ( TOF ) analysis transformed IM-MS into a powerful probe for biomolecules nearly three decades later [4–6]. Despite lower resolution than methods such as high-performance liquid chromatography ( HPLC ), IM-MS has found increasing analytical utility and applications as evidenced by extensive literature [7–9].…”

Section: Introductionmentioning

confidence: 99%

Large-Scale Collision Cross-Section Profiling on a Traveling Wave Ion Mobility Mass Spectrometer

Lietz

Li³

2014

J. Am. Soc. Mass Spectrom.

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Ion mobility (IM) is a gas-phase electrophoretic method that separates ions according to charge and ion-neutral collision cross-section (CCS). Herein, we attempt to apply a travelling wave (TW) IM polyalanine calibration method to shotgun proteomics and create a large peptide CCS database. Mass spectrometry methods that utilize IM, such as HDMSE, often use high transmission voltages for sensitive analysis. However, polyalanine calibration has only been demonstrated with low voltage transmission used to prevent gas-phase activation. If polyalanine ions change conformation under higher transmission voltages used for HDMSE, the calibration may no longer be valid. Thus, we aimed to characterize the accuracy of calibration and CCS measurement under high transmission voltages on a TW IM instrument using the polyalanine calibration method and found that the additional error was not significant. We also evaluated the potential error introduced by liquid chromatography (LC)-HDMSE analysis, and found it to be insignificant as well, validating the calibration method. Finally, we demonstrated the utility of building a large-population peptide CCS database by investigating the effects of terminal lysine position, via LysC or LysN digestion, on the formation of two structural sub-families formed by triply charged ions.

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Section: Introductionmentioning

confidence: 99%

Large-Scale Collision Cross-Section Profiling on a Traveling Wave Ion Mobility Mass Spectrometer

Lietz

Li³

2014

J. Am. Soc. Mass Spectrom.

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“…In the 1960s and 70s, a transition occurred from using IMS primarily as a fundamental physics research tool to using it as a separations device for analytical and physical chemistry applications. Notably, the early 1960s also marked the first reports of combining IMS with MS (IM-MS) [8,9].On the basis of these early IM-MS instruments, it was proposed that with proper calibration, IMS instruments could be operated as atmospheric pressure mass spectrometers in that mass could be assigned to a particular IM drift time [10,11]. This supposition was derived from plotting curves of mass as a function of mobility, which resulted in highly correlated calibration curves.…”

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confidence: 99%

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The mass-mobility correlation redux: The conformational landscape of anhydrous biomolecules

McLean

2009

J. Am. Soc. Mass Spectrom.

100

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Structural separations on the basis of gas-phase ion mobility-mass spectrometry are increasingly used for the analysis of complex biological samples. As a tool to elucidate biomolecular structure, ion mobility-mass spectrometry methods are unique in that direct molecular structural information is obtained for all resolved species, largely irrespective of the complexity of the sample. Computational approaches are used to interpret and discern structural details consistent with the empirical results. To a first approximation, correlations of mobility with mass allow for qualitative identification of the molecular class to which a particular species belongs. These correlations allow simultaneous characterization of different classes of biomolecules, which provides a means for combining omics measurements, such as lipidomics, proteomics, glycomics, and metabolomics, in the same analysis. Examination of the correlation of fine structure reveals that specific structural motifs, chemical functionality, chemical connectivity, and composition may also be determined, depending on the specific biomolecular class. Mapping the coarse and fine structure in ion mobility-mass spectrometry conformation space measurements provides an atlas for interpretation and discovery in complicated spectra. as-phase separations on the basis of migration and diffusion of ions through a neutral gas under the influence of an applied field have existed for over a century. The first examples of gasphase ion mobility (IM) include the quantitative studies of ionized gases by Rutherford shortly after the discovery of X-rays [1,2]. To place these early IM experiments in the context of mass spectrometry (MS), it would be almost another decade before J. J. Thomson would construct his first mass spectrograph [3]. Over the historic span of IMS development, the technique has been referred to by several names, including plasma chromatography [4], ion chromatography [5], and the currently accepted term ion mobility spectrometry (IMS). A detailed account on the historic development of IMS and milestones in the progress of gas-phase IM techniques is described elsewhere [6,7]. For many years, IMS separations were used for the fundamental study of atomic and small molecular ions in plasma physics. In the 1960s and 70s, a transition occurred from using IMS primarily as a fundamental physics research tool to using it as a separations device for analytical and physical chemistry applications. Notably, the early 1960s also marked the first reports of combining IMS with MS (IM-MS) [8,9].On the basis of these early IM-MS instruments, it was proposed that with proper calibration, IMS instruments could be operated as atmospheric pressure mass spectrometers in that mass could be assigned to a particular IM drift time [10,11]. This supposition was derived from plotting curves of mass as a function of mobility, which resulted in highly correlated calibration curves. However, this notion was qualified by Horning and colleagues in that highly correlated mass-mobility relat...

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“…Ionization (a) and attachment (n) coefficients of SF6' Experiment: X -Geballe and Harrison [16],0 -Bhalla and Craggs [17],\1-McAfee and Edelson [18], 6. - Maller and Naidu [19 J , (P20; 1 torr).…”

Section: Evaluation Of the Cross Sectionsmentioning

confidence: 99%

Insulating properties of mixtures of nitrogen with electronegative gases

Novák

Fréchette

1984

1984 IEEE International Conference on Eletrical Insulation

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Calculations of the transport coefficients of insulating electronegative gases and their mixtures were performed under the conditions of the Townsend steadystate experiment.The Boltzmann equation was used for evaluation of the unknown collision cross sections by fitting calculated ionization coefficients, drift velocities and diffusion coefficients to experimental data.A stainless-steel vacuum chamber (lO-s torr), provided with a pair of Rogowski-profile electrodes, was set up and used to carry out a series of measurements. The ionization and attachment coefficients were evaluated from the steady-state prebreakdown currents. Results for SF6 are presented in this paper.

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Identification and Mobility of Ions in a Townsend Discharge by Time-resolved Mass Spectrometry

Cited by 79 publications

References 9 publications

Large-Scale Collision Cross-Section Profiling on a Traveling Wave Ion Mobility Mass Spectrometer

Large-Scale Collision Cross-Section Profiling on a Traveling Wave Ion Mobility Mass Spectrometer

The mass-mobility correlation redux: The conformational landscape of anhydrous biomolecules

Insulating properties of mixtures of nitrogen with electronegative gases

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