Towards measuring ion mobilities in non-stationary gases and non-uniform and dynamic electric fields (I). Transport equation

Bleiholder, Christian

doi:10.1016/j.ijms.2016.01.003

Cited by 28 publications

(44 citation statements)

References 37 publications

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“…For TWIMS and TIMS, in practice the K 0 and CCS values are determined via an instrumental calibration function f determined using reference compounds. With TIMS (Bleiholder, ) and TWIMS (Giles et al, ; Mortensen et al, ; Mortensen, Susa, & Williams, ; Richardson, Langridge, & Giles, ), obtaining K 0 without calibration may be achievable in principle, but the uncertainty associated with such approaches in development has not yet been fully evaluated. In DMA measurements, precise knowledge of the applied voltage, DMA dimensions, and fluid flow rates into the device can yield K 0 values without the need for calibration.…”

Section: Classification Of Im‐ms Methodsmentioning

confidence: 99%

“…In a TIMS analyzer, the axial electric field E varies both temporally and spatially (Fernandez‐Lima et al, ; Michelmann et al, ; Bleiholder, ). Spatially, the electric field strength increases over the length of the ion storage region up to a value E 0 in the first half of the analyzer (“ramp”) whereas it remains constant at E 0 in the second half of the analyzer (“plateau”).…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

“…Temporally, this electric field profile is controlled by the rate β at which the plateau height E 0 is decreased (“ramp rate”). Mathematically, the electric field strength at axial location z in the analyzer at time t is given by (Michelmann et al, ; Bleiholder, ):

E true(z, t true) = true{\begin{array}{c} center & s true(z true) true(E_{0} - β t true); \forall z < z_{0} \\ center & E_{0} - β t; \forall z \geq z_{0} \end{array}

where z 0 denotes the location of the center in the TIMS analyzer, s ( z ) is a function that describes how the electric field strength increases over the length of the first half of the analyzer, and β is the electric field scan rate. The function s ( z ) depends on the exact configuration of the resistor chain that connects the electrodes in the analyzer region.…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

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Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

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370

477

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Here we present a guide to ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties of mobility and collision cross section values. The guide aims to clarify some possibly confusing concepts, and the reporting recommendations should help researchers, authors and reviewers to contribute comprehensive reports, so that the ion mobility data can be reused more confidently. Starting from the concept of the definition of the measurand, we emphasize that (i) mobility values ( K 0 ) depend intrinsically on ion structure, the nature of the bath gas, temperature, and E / N ; (ii) ion mobility does not measure molecular surfaces directly, but collision cross section (CCS) values are derived from mobility values using a physical model; (iii) methods relying on calibration are empirical (and thus may provide method‐dependent results) only if the gas nature, temperature or E / N cannot match those of the primary method. Our analysis highlights the urgency of a community effort toward establishing primary standards and reference materials for ion mobility, and provides recommendations to do so. © 2019 The Authors. Mass Spectrometry Reviews Published by Wiley Periodicals, Inc.

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Section: Classification Of Im‐ms Methodsmentioning

confidence: 99%

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

E true(z, t true) = true{\begin{array}{c} center & s true(z true) true(E_{0} - β t true); \forall z < z_{0} \\ center & E_{0} - β t; \forall z \geq z_{0} \end{array}

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

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Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

Self Cite

370

477

View full text Add to dashboard Cite

show abstract

“…Such pressures correspond to mean free paths between collisions of approximately 0.4 μm to 0.1 μm. At FSU, where we carry out measurements at ~3 mbar in nitrogen buffer gas (50,51), the mean free path is in the order of 0.6 μm. In travelling-wave instruments, which are typically operated at 0.5mbar to 1mbar (49), mean free paths are on the order of 3.6 μm, resulting in energy transfer that is ~36 and ~1237 more effective than in our TIMS setup at FSU and the high-resolution drift tube at UCSB, respectively.…”

Section: Softness Of Ims-ms Measurements: the Ability To Study Biologmentioning

confidence: 99%

“…In these instruments, mass analysis occurs in a quadrupole directly attached to the IMS drift tube, effectively preventing any reactions of the assemblies to take place between IMS and mass analysis. In the trapped IMS system used at FSU ions traverse a quadrupole and a collision cell between IMS and mass analysis (45,46,50,51). We find that the presence of triply-charged bradykinin trimers depends significantly on the energy used to injected the assemblies into the collision cell (not shown).…”

Section: Softness Of Ims-ms Measurements: the Ability To Study Biologmentioning

confidence: 99%

The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Bleiholder

Bowers

2017

Annual Rev. Anal. Chem.

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Ion mobility spectrometry-mass spectrometry (IMS-MS) methods are increasingly used to study noncovalent assemblies of peptides and proteins. This review focuses on the noncovalent self-assembly of amino acids and peptides, systems at the heart of the amyloid process that play a central role in a number of devastating diseases. Three different systems are discussed in detail: the 42-residue peptide amyloid-β42 implicated in the etiology of Alzheimer's disease, several amyloid-forming peptides with 6–11 residues, and the assembly of individual amino acids. We also discuss from a more fundamental perspective the processes that determine how quickly proteins and their assemblies denature when the analyte ion has been stripped of its solvent in an IMS-MS measurement and how to soften the measurement so that biologically meaningful data can be recorded.

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Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

Perchepied,

Zhou,

Mitulović

et al. 2023

J of Separation Science

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Ion mobility spectrometry‐mass spectrometry (IMS‐MS) is experiencing rapid growth in proteomic studies, driven by its enhancements in dynamic range and throughput, increasing the quantitation precision, and the depth of proteome coverage. The core principle of ion mobility spectrometry is to separate ions in an inert gas under the influence of an electric field based on differences in drift time. This minireview provides an introduction to IMS operation modes and a description of advantages and limitations is presented. Moreover, the principles of trapped IMS‐MS (TIMS‐MS), including parallel accumulation‐serial fragmentation are discussed. Finally, emerging applications linked to TIMS focusing on sample throughput (in clinical proteomics) and sensitivity (single‐cell proteomics) are reviewed, and the possibilities of intact protein analysis are discussed.

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Towards measuring ion mobilities in non-stationary gases and non-uniform and dynamic electric fields (I). Transport equation

Cited by 28 publications

References 37 publications

Recommendations for reporting ion mobility Mass Spectrometry measurements

Recommendations for reporting ion mobility Mass Spectrometry measurements

The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

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