Ion Mobility‐Mass Spectrometry

Jiang, Wentao; Robinson, Renã A. S.

doi:10.1002/9780470027318.a9292

Cited by 7 publications

(5 citation statements)

References 183 publications

(200 reference statements)

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“…CCS calculation is based on the extended Mason–Schamp equation:

normalΩ = \frac{{((), 18 π)}^{1 / 2}}{16 N} \frac{z e}{{((), k_{b} T)}^{1 / 2}} {[\frac{1}{m_{ion}} + \frac{1}{m_{gas}}]}^{1 true/ 2} \frac{760}{P} \frac{T}{273} \frac{V}{L^{2}} t_{d}

where Ω is the CCS of the analyte ion, e is the charge on an electron, z is the state charge of the analyte ion, k b is the Boltzmann constant, N is the number density of the drift gas, T is the temperature, P is the drift gas pressure, V is the drift voltage, which is the voltage difference between the entrance and exit of the drift region, L is the flight tube length, and m gas and m ion are the molecular masses of the drift gas and analyte ion, respectively. Because MS is coupled to IMS, the mass and charge of the analyte ion ( m ion , z ) can be readily deduced.…”

Section: Methodsmentioning

confidence: 99%

Characterizing ion mobility and collision cross section of fatty acids using electrospray ion mobility mass spectrometry

Zhang

Guo

Zhang³

et al. 2015

J. Mass Spectrom.

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This study investigated the ion mobility (IM) and the collision cross section (CCS) of fatty acids (FAs) using electrospray IM MS. The IM analysis of 18 FA ions showed intriguing differences among the saturated FAs, monounsaturated FAs, multi-unsaturated FAs, and cis-isomer/trans-isomer with respect to the aliphatic tail chains. The length of aliphatic tail chain present in the ion structures had a strong influence on the differentiation of drift, while the number of double bond showed a weaker influence. The tiny drift differences between cis-isomer and trans-isomer were also observed. In the CCS measurements, two internal standards were involved in the mobility calibration and accuracy estimation. It insured our empirical CCS values were of high experimental precision (±0.35% or better) and accuracy (±0.25% or better). Moreover, the mass-to-charge ratio (m/z) - mobility plots obtained by ion mobility spectrometry with mass spectrometry analysis of FAs - was used to investigate the structural relationship between the molecules. Each series of FAs sharing a similar structure was aligned in the linear plot. Finally, the developed procedure was applied to the determination of FAs in rat adipose tissues, and it allowed the presence of 13 FAs to be confirmed with their exact masses and CCS values. These studies reveal the direct relationship between the behaviors in IM and the molecular structures and thus may provide further validations to the FA identification process.

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“…CCS calculation is based on the extended Mason–Schamp equation:

normalΩ = \frac{{((), 18 π)}^{1 / 2}}{16 N} \frac{z e}{{((), k_{b} T)}^{1 / 2}} {[\frac{1}{m_{ion}} + \frac{1}{m_{gas}}]}^{1 true/ 2} \frac{760}{P} \frac{T}{273} \frac{V}{L^{2}} t_{d}

Section: Methodsmentioning

confidence: 99%

Characterizing ion mobility and collision cross section of fatty acids using electrospray ion mobility mass spectrometry

Zhang

Guo

Zhang³

et al. 2015

J. Mass Spectrom.

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“…In contrast to a mass spectrometer (MS), an IMS does not separate ions by mass-to-charge ratio but mainly by ion–neutral collision cross section depending on the ion size and structure . Therefore, an IMS is often coupled with an MS to obtain an additional separation dimension and additional information about the ions besides the mass-to-charge ratio. , …”

Section: Introductionmentioning

confidence: 99%

Ion Mobility Shift of Isotopologues in a High Kinetic Energy Ion Mobility Spectrometer (HiKE-IMS) at Elevated Effective Temperatures

Schaefer

Kirk

Allers

et al. 2020

J. Am. Soc. Mass Spectrom.

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Ion mobility spectrometers (IMS) separate ions mainly by ion-neutral collision cross section and to a lesser extent by ion mass and effective temperature. When investigating isotopologues, the difference in collision cross section can be assumed negligible. Since the mobility shift of isotopologues is thus mainly caused by their difference in mass and effective temperature the investigation of isotopologues can provide important insights into the theory of ion mobility. However, in classical IMS operated at ambient pressure, cluster formation with neutral molecules occurs, which significantly influences the mobility shift of isotopologues and thus makes a sound investigation of the effect of ion mass and effective temperature on the ion mobility difficult. In this work, the relative ion mobility of several organic compounds and their 13 C-labelled isotopologues is studied in a High Kinetic Energy Ion Mobility Spectrometer (HiKE-IMS) at high reduced electric fields up to 120 Td, which allows the investigation of non-clustered ion species and thus enables a sound investigation of the mobility shift of isotopologues. The results show that the measured relative ion mobilities of isotopologues having the same effective temperature, and thus their ion mass dominating the relative ion mobility, agree well with theoretical relative ion mobilities predicted by the theory of ion mobility.

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“…Recently, a number of ion mobility separation (IMS-MS) platforms have been launched by major MS vendors . IMS is a group of techniques that fractionates ions based on the velocity of movement through buffer gas in an electric field . Importantly, ion mobility separation occurs within the hybrid IMS-MS platform and does not require an increase in instrument time.…”

Section: Introductionmentioning

confidence: 99%

Additional Precursor Purification in Isobaric Mass Tagging Experiments by Traveling Wave Ion Mobility Separation (TWIMS)

et al. 2014

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Despite the increasing popularity of data-independent acquisition workflows, data-dependent acquisition (DDA) is still the prevalent method of LC-MS-based proteomics. DDA is the basis of isobaric mass tagging technique, a powerful MS2 quantification strategy that allows coanalysis of up to 10 proteomics samples. A well-documented limitation of DDA, however, is precursor coselection, whereby a target peptide is coisolated with other ions for fragmentation. Here, we investigated if additional peptide purification by traveling wave ion mobility separation (TWIMS) can reduce precursor contamination using a mixture of Saccharomyces cerevisiae and HeLa proteomes. In accordance with previous reports on FAIMS-Orbitrap instruments, we find that TWIMS provides a remarkable improvement (on average 2.85 times) in the signal-to-noise ratio for sequence ions. We also report that TWIMS reduces reporter ions contamination by around one-third (to 14-15% contamination) and even further (to 6-9%) when combined with a narrowed quadrupole isolation window. We discuss challenges associated with applying TWIMS purification to isobaric mass tagging experiments, including correlation between ion m/z and drift time, which means that coselected peptides are expected to have similar mobility. We also demonstrate that labeling results in peptides having more uniform m/z and drift time distributions than observed for unlabeled peptides. Data are available via ProteomeXchange with identifier PXD001047.

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Ion Mobility‐Mass Spectrometry

Cited by 7 publications

References 183 publications

Characterizing ion mobility and collision cross section of fatty acids using electrospray ion mobility mass spectrometry

Characterizing ion mobility and collision cross section of fatty acids using electrospray ion mobility mass spectrometry

Ion Mobility Shift of Isotopologues in a High Kinetic Energy Ion Mobility Spectrometer (HiKE-IMS) at Elevated Effective Temperatures

Additional Precursor Purification in Isobaric Mass Tagging Experiments by Traveling Wave Ion Mobility Separation (TWIMS)

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