Trapped ion mobility spectrometry: A short review

Ridgeway, Mark E.; Lubeck, Markus; Jordens, Jan; Mann, Matthias; Park, Melvin A.

doi:10.1016/j.ijms.2018.01.006

Cited by 265 publications

(260 citation statements)

References 70 publications

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“…A variety of commercial IMS‐MS instruments have been released to meet the demand for ion mobility analysis. Most of these couple a time‐of‐flight (TOF) MS analyzer with one of various ion mobility techniques, including linear Drift Tube Ion Mobility (DT‐IMS), Travelling Wave IMS (TW‐IMS), and Trapped Ion Mobility Spectrometry (TIMS) . All of these techniques employ ion mobility at reduced pressure to achieve compatibility with the vacuum regime of the TOF instrument.…”

Section: Introduction: Instrumentation Highlightsmentioning

confidence: 99%

Separation of biologically relevant isomers on an Orbitrap mass spectrometer using high‐resolution drift tube ion mobility and varied drift gas mixtures

Kaszycki

Rotta

Colsch

et al. 2019

Rapid Comm Mass Spectrometry

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Rationale Atmospheric pressure drift tube ion mobility is a powerful addition to the Orbitrap mass spectrometer enabling direct separation of isomers. Apart from offering high resolving power in a compact design, it also facilitates optimization of the separation gas, as shown here for a series of biologically relevant isomer pairs. Methods An Excellims MA3100 High‐Resolution Atmospheric Pressure Ion Mobility Spectrometer (HR‐IMS) was coupled to a Thermo Scientific™ Q Exactive™ Focus hybrid quadrupole–Orbitrap™ mass spectrometer, using an Excellims Directspray™ Electrospray Ionization source and a gas mixture setup to provide various drift gases (air, CO2 and mixtures). This instrument combination was used to separate isomers of eight pairs of metabolites and gangliosides, optimizing drift gas conditions for best separation of each set. Results All but one of the isomers pairs provided could be partially or fully separated by the HR‐IMS‐MS combination using ion mobility drift times. About half of the separated compounds showed significantly better analytical separation when analyzed in a mixture of CO2 and air rather than air or CO2 alone. Resolving power of up to 102 was achieved using the 10 cm atmospheric drift tube ion mobility add‐on for the Orbitrap mass spectrometer. Conclusions The present analysis demonstrates the usefulness of using atmospheric drift tube IMS on an Orbitrap mass spectrometer to characterize the isomeric composition of samples. It also highlights the potential benefits of being able to quickly optimize the drift gas composition to selectively maximize the mobility difference for isomer separation.

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Section: Introduction: Instrumentation Highlightsmentioning

confidence: 99%

Separation of biologically relevant isomers on an Orbitrap mass spectrometer using high‐resolution drift tube ion mobility and varied drift gas mixtures

Kaszycki

Rotta

Colsch

et al. 2019

Rapid Comm Mass Spectrometry

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“…Improvements in time of flight and other enhanced MS platforms have also complemented the recent MS revolution. Along with advances in mass analyzer technology, ion mobility spectrometry (IMS) was introduced to resolve analytes of equal mass (eg, isomers) prior to MS. Ion mobility exists in multiple formats including drift time IMS (DTIMS), high field asymmetric waveform IMS (FAIMS), trapped IMS (TIMS), or travelling Wave IMS (TWIMS) . Being integrated into commercial MS platforms, IMS is used to enhance proteome isolation and characterization .…”

Section: The Proteomics Facility: Instrumentationmentioning

confidence: 99%

Developing front‐end devices for improved sample preparation in MS‐based proteome analysis

Doucette

Nickerson

2020

J Mass Spectrom

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Chemical analysis has long relied on instrumentation, from the simplest (eg, burets) to the more sophisticated (eg, mass spectrometers) to facilitate precision measurements. Regardless of their complexity, the development of a new instrumental device can be a valued approach to address problems in science. In this perspective, we outline the process of novel device design, from early phase conception to the manufacturing and testing of the tool or gadget. Focus is placed on the development of improved front‐end devices to facilitate protein sample manipulations ahead of mass spectrometry, which therefore augment the proteomics workflow. Highlighted are some of the many training secrets, choices, and challenges that are inherent to the often iterative process of device design. In hopes of inspiring others to pursue instrument design to address relevant research questions, we present a summary list of points to consider prior to innovating their own devices.

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“…For biomacromolecules, the IM separation technologies available for quantitative size determination are essentially of four types; drift tube, travelling wave, trapped ion and differential mobility analyzers. Aspects of these IM‐MS techniques and their applications have been described in detail in several recent notable reviews . Consequently, only a brief summary of these IM separation approaches is provided here.…”

Section: Basic Principles Of Ccs Measurementmentioning

confidence: 99%

“…Following the trapping event, ions are sequentially eluted with ascending mobilities by gradually reducing the electric field strength. A key advantage of this approach is that the physical dimensions of the IM cell can be significantly reduced (approximately 5 cm) while achieving high resolving power (R ∼ 300), duty cycle (100%), and efficiency (∼80%) . Importantly, the fundamental physics of TIMS is the same as that in DTIMS and the relationship between mobility and CCS still applies; hence, it is possible to measure ion CCS using first principles for structural characterization.…”

Section: Basic Principles Of Ccs Measurementmentioning

confidence: 99%

Importance of collision cross section measurements by ion mobility mass spectrometry in structural biology

Pukala

2019

Rapid Comm Mass Spectrometry

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The field of ion mobility mass spectrometry (IM‐MS) has developed rapidly in recent decades, with new fundamental advances underpinning innovative applications. This has been particularly noticeable in the field of biomacromolecular structure determination and structural biology, with pioneering studies revealing new structural insight for complex protein assemblies which control biological function. This perspective offers a review of recent developments in IM‐MS which have enabled expanding applications in protein structural biology, principally focusing on the quantitative measurement of collision cross sections and their interpretation to describe higher order protein structures.

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Trapped ion mobility spectrometry: A short review

Cited by 265 publications

References 70 publications

Separation of biologically relevant isomers on an Orbitrap mass spectrometer using high‐resolution drift tube ion mobility and varied drift gas mixtures

Separation of biologically relevant isomers on an Orbitrap mass spectrometer using high‐resolution drift tube ion mobility and varied drift gas mixtures

Developing front‐end devices for improved sample preparation in MS‐based proteome analysis

Importance of collision cross section measurements by ion mobility mass spectrometry in structural biology

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