Trapped Ion Mobility Spectrometry: past, present and future trends

Fernandez-Lima, Francisco

doi:10.1007/s12127-016-0206-3

Cited by 13 publications

(8 citation statements)

References 24 publications

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“…An overview of the TIMS instrument and its operating principles can be found elsewhere (see Figure S1, supporting information) . In TIMS‐MS operation, ions are held stationary against a flow of bath gas by a variable electric field applied along the length of the TIMS tunnel, resulting in ions being simultaneously trapped at different axial positions according to their mobility.…”

Section: Methodsmentioning

confidence: 99%

“…An overview of the TIMS instrument and its operating principles can be found elsewhere (see Figure S1, supporting information). 14,18,19 In TIMS-MS operation, ions are held stationary against a flow of bath gas by a variable electric field applied along the length of the TIMS tunnel, resulting in ions being simultaneously trapped at different axial positions according to their mobility. The voltage of the tunnel is then ramped to elute ions from the TIMS analyzer, after which they are mass analyzed and detected by a maXis impact Q-TOF mass spectrometer (Bruker Daltonics Inc., Billerica, MA, USA).…”

Section: Trapped Ion Mobility Spectrometry-mass Spectrometry Analysismentioning

confidence: 99%

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The effects of solution additives and gas‐phase modifiers on the molecular environment and conformational space of common heme proteins

Butcher

Mikšovská

Ridgeway

et al. 2019

Rapid Comm Mass Spectrometry

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Rationale The molecular environment is known to impact the secondary and tertiary structures of biomolecules both in solution and in the gas phase, shifting the equilibrium between different conformational and oligomerization states. However, there is a lack of studies monitoring the impacts of solution additives and gas‐phase modifiers on biomolecules characterized using ion mobility techniques. Methods The effect of solution additives and gas‐phase modifiers on the molecular environment of two common heme proteins, bovine cytochrome c and equine myoglobin, is investigated as a function of the time after desolvation (e.g., 100–500 ms) using nanoelectrospray ionization coupled to trapped ion mobility spectrometry with detection by time‐of‐flight mass spectrometry. Organic compounds used as additives/modifiers (methanol, acetonitrile, acetone) were either added to the aqueous protein solution before ionization or added to the ion mobility bath gas by nebulization. Results Changes in the mobility profiles are observed depending on the starting solution composition (i.e., in aqueous solution at neutral pH or in the presence of organic content: methanol, acetone, or acetonitrile) and the protein. In the presence of gas‐phase modifiers (i.e., N2 doped with methanol, acetone, or acetonitrile), a shift in the mobility profiles driven by the gas‐modifier mass and size and changes in the relative abundances and number of IMS bands are observed. Conclusions We attribute the observed changes in the mobility profiles in the presence of gas‐phase modifiers to a clustering/declustering mechanism by which organic molecules adsorb to the protein ion surface and lower energetic barriers for interconversion between conformational states, thus redefining the free energy landscape and equilibria between conformers. These structural biology experiments open new avenues for manipulation and interrogation of biomolecules in the gas phase with the potential to emulate a large suite of solution conditions, ultimately including conditions that more accurately reflect a variety of intracellular environments.

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Section: Methodsmentioning

confidence: 99%

Section: Trapped Ion Mobility Spectrometry-mass Spectrometry Analysismentioning

confidence: 99%

The effects of solution additives and gas‐phase modifiers on the molecular environment and conformational space of common heme proteins

Butcher

Mikšovská

Ridgeway

et al. 2019

Rapid Comm Mass Spectrometry

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“…TIMS-FTICR MS was recently deployed for the description of petroleum and other complex natural mixtures. [11][12][13] To the best of the author's knowledge, this is the first proof of principle study addressing a planetary science subject. As an example, the soluble fraction of a tholins sample is investigated by electrospray ionization (ESI) coupled to TIMS-FTICR MS.…”

mentioning

confidence: 93%

Structural Study of Analogues of Titan’s Haze by Trapped Ion Mobility Coupled with a Fourier Transform Ion Cyclotron Mass Spectrometer

Rueger

Maillard

Maitre

et al. 2019

J. Am. Soc. Mass Spectrom.

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The aerosols present in the atmosphere of the Saturn's moon Titan are of particular planetary science interest and several spacecraft missions already allowed to gather spectroscopic data. Titan haze's analogs, so-called tholins, were produced on earth to push forward the comprehension of their formation and properties. In this study, this highly complex mixture was analyzed here for the first time by trapped ion mobility spectrometry coupled to ultra-high resolution mass spectrometry (FTICR MS). Electrospray ionization revealed the characteristic CHN x -class components, with CHN 5-6 and DBE 6-7 most abundant. Deploying specialized visualization, enabled by accurate mass measurements and elemental composition assignments, the adapted Kendrick mass defect analysis highlights the C 2 H 3 N homolog series, whereas the nitrogen-modified van Krevelen diagram exhibits a clear trend towards H/C 1.5 and N/C 0.5. More interestingly, the representation of m/z versus collision cross section (CCS) allowed hypothesizing a ramified N-PAH structural motif. State-of-the-art IMS is currently not able to resolve the isomeric continuum of ultra-complex mixtures; thus peak parameter other than the CCS-value are explored. As such, analyzing the mobility peak width versus m/z shows a linear increase in isomeric diversity between m/z 170 and 350 and a near plateau in diversity at higher m/z for the N-PAH-like structure. Due to the high complexity of the sample, these structural insights are only to be revealed by TIMS-FTICR MS.

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“…The operation of the TIMS cell (Figure S2) has been described elsewhere. − The nitrogen bath gas flow is defined by the pressure differential between the entrance funnel ( P 1 = 2.6 mbar) and the exit funnel ( P 2 = 1.1 mbar) at ca. 293 K. A 880 kHz and 200 V pp rf trapping potential was applied.…”

Section: Methodsmentioning

confidence: 99%

Differentiating Parallel and Antiparallel DNA Duplexes in the Gas Phase Using Trapped Ion Mobility Spectrometry

et al. 2018

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Deoxyribonucleic acids can form a wide variety of structural motifs which differ greatly from the typical antiparallel duplex stabilized by Watson-Crick base pairing. Many of these structures are thought to occur in vivo and may have essential roles in the biology of the cell. Among these is the parallel-stranded duplex-a structural motif in which DNA strands associate in a head-to-head fashion with the 5' ends at the same end of the duplex-which is stabilized by reverse Watson-Crick base pairing. In this study, parallel- and antiparallel-stranded DNA duplexes formed from two different 12-mer oligonucleotides were studied using native electrospray ionization combined with trapped ion mobility spectrometry and mass spectrometry. The DNA duplex charge plays an important role in the gas-phase mobility profile, with a more compact form in negative mode than in positive mode (ΔΩ ≈ 100 Å between -4 and +4). Despite sequence mismatches, homo- and hetero-DNA duplexes were formed in solution and transfer to the gas phase, where a more compact structure was observed for the parallel compared to the antiparallel duplexes (ΔΩ ≈ 50 Å), in good agreement with theoretical calculations. Theoretical studies suggest that a reduction (or compaction) along the helical axis of the parallel and antiparallel DNA duplexes is observed upon transfer to the gas phase.

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Trapped Ion Mobility Spectrometry: past, present and future trends

Cited by 13 publications

References 24 publications

The effects of solution additives and gas‐phase modifiers on the molecular environment and conformational space of common heme proteins

The effects of solution additives and gas‐phase modifiers on the molecular environment and conformational space of common heme proteins

Structural Study of Analogues of Titan’s Haze by Trapped Ion Mobility Coupled with a Fourier Transform Ion Cyclotron Mass Spectrometer

Differentiating Parallel and Antiparallel DNA Duplexes in the Gas Phase Using Trapped Ion Mobility Spectrometry

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