Validation of Calibration Parameters for Trapped Ion Mobility Spectrometry

Naylor, Cameron N.; Reinecke, Tobias; Ridgeway, Mark E.; Park, Melvin A.; Clowers, Brian H.

doi:10.1007/s13361-019-02289-1

Cited by 28 publications

(48 citation statements)

References 50 publications

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“…These are the K 0 values recommended by the manufacturer and in close agreement with others reported in the literature (see details in Table S1). − Values of K 0 were correlated with the ion-neutral collision cross section (Ω, Å 2 ) using the Mason–Schamp equation: where z is the charge of the ion, k B is the Boltzmann constant, m 1 is the ion mass, m b is the bath gas molecule mass, T is the temperature (305 K), and N ★ is the gas number density.…”

Section: Methodsmentioning

confidence: 99%

Comprehensive Screening of Polycyclic Aromatic Hydrocarbons and Similar Compounds Using GC–APLI–TIMS–TOFMS/GC–EI–MS

2021

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In the present work, a novel workflow based on complementary gas-phase separations for the identification of isomeric PAHs from complex mixtures is described. This is the first report on the coupling of gas chromatography (GC), atmospheric pressure laser ionization (APLI), and trapped ion mobility spectrometry–mass spectrometry (TIMS–MS) for the characterization of polycyclic aromatic hydrocarbons. Over a hundred known unknowns are uniquely identified based on the molecular ion retention indices I (5%), mobility (RSD < 0.6% and R = 50–90 with S r = 0.18 V/ms), mobility-based theoretical candidate assignment (<3%), accurate mass chemical formula assignment (<2 ppm), and electron impact fragmentation pattern and database search. The advantages of theoretical modeling of PAHs and similar compounds were evaluated using candidate structures ranked by retention indices and fragmentation pattern from GC–EI–MS data sets. Over 20 PAH isomeric and deuterated standards were utilized for the GC–APLI–TIMS–TOF MS workflow validation. Noteworthy is the analytical capability for untargeted screening of isomeric and isobaric compounds with additional characterization metrics not available in traditional GC–EI–MSn workflows.

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Section: Methodsmentioning

confidence: 99%

Comprehensive Screening of Polycyclic Aromatic Hydrocarbons and Similar Compounds Using GC–APLI–TIMS–TOFMS/GC–EI–MS

2021

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“…The timsTOF Pro calibration was performed using a low-concentration ESI tune mix (P/N G1969–85010, Agilent Technologies, Santa Clara, CA,) as described previously. , Nitrogen was the buffer gas for all measurements. Following the instrument calibration, the standard ESI source was replaced by a custom, lab-built CE–ESI source and the acquisition was adjusted to the optimized TIMS MS method.…”

Section: Methodsmentioning

confidence: 99%

Analysis of Peptide Stereochemistry in Single Cells by Capillary Electrophoresis–Trapped Ion Mobility Spectrometry Mass Spectrometry

et al. 2021

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Single cell analysis strives to probe molecular heterogeneity in morphologically similar cell populations through quantitative or qualitative measurements of genetic, proteomic, or metabolic products. Here, we applied mass analysis of single neurons to investigate cell–cell signaling peptides. The multiplicity of endogenous cell–cell signaling peptides is a common source of chemical diversity among cell populations. Certain peptides can undergo post-translational isomerization of select residues, which has important physiological consequences. The limited number of single cell analysis techniques that are sensitive to peptide stereochemistry make it challenging to study isomerization at the individual cell level. We performed capillary electrophoresis (CE) with mass spectrometry (MS) detection to characterize the peptide content of single cells. Using complementary trapped ion mobility spectrometry (TIMS) separations, we measured the stereochemical configurations of three neuropeptide gene products derived from the pleurin precursor in individual neurons (N = 3) isolated from the central nervous system of Aplysia californica. An analysis of the resultant mobility profiles indicated >98% of the detectable pleurin-derived peptides exist as the nonisomerized, all-l forms in individual neuron cell bodies. However, we observed 44% of the Plrn2 peptide from the pleurin precursor was present as the isomerized, d-residue-containing form in the nerve tissue. These findings demonstrate an unusual distribution of isomerized peptides in A. californica and establish CE–TIMS MS as a powerful analytical tool for investigating peptide stereochemistry at the single cell level.

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“…Similar to TWIM, the CCS is then determined after calibration. [145][146][147][148] IM adds another dimension of separation during native MS analysis of proteins and protein complexes; ions with the same m/z but differing in shape can be distinguished and structurally characterized ( Figure 9D). A key finding was the observation that the ring structure of the tRNA binding protein TRAP was maintained in the gas phase evidencing the applicability of native IM-MS for studying protein complex structures.…”

Section: Assessing Protein Shape and Stability Through Native Im-msmentioning

confidence: 99%

“…When compared with other IM techniques, analytes with low mobility and extended shape are released first because they undergo more collisions with the buffer gas. Similar to TWIM, the CCS is then determined after calibration 145–148 …”

Section: Assessing Protein Shape and Stability Through Native Im‐msmentioning

confidence: 99%

Native mass spectrometry—A valuable tool in structural biology

Barth

Schmidt

2020

J Mass Spectrom

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Proteins and the complexes they form with their ligands are the players of cellular action. Their function is directly linked with their structure making the structural analysis of protein-ligand complexes essential. Classical techniques of structural biology include X-ray crystallography, nuclear magnetic resonance spectroscopy and recently distinguished cryo-electron microscopy. However, protein-ligand complexes are often dynamic and heterogeneous and consequently challenging for these techniques. Alternative approaches are therefore needed and gained importance during the last decades. One alternative is native mass spectrometry, which is the analysis of intact protein complexes in the gas phase. To achieve this, sample preparation and instrument conditions have to be optimised. Native mass spectrometry then reveals stoichiometry, protein interactions and topology of protein assemblies. Advanced techniques such as ion mobility and high-resolution mass spectrometry further add to the range of applications and deliver information on shape and microheterogeneity of the complexes. In this tutorial, we explain the basics of native mass spectrometry including sample requirements, instrument modifications and interpretation of native mass spectra. We further discuss the developments of native mass spectrometry and provide example spectra and applications.

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Validation of Calibration Parameters for Trapped Ion Mobility Spectrometry

Cited by 28 publications

References 50 publications

Comprehensive Screening of Polycyclic Aromatic Hydrocarbons and Similar Compounds Using GC–APLI–TIMS–TOFMS/GC–EI–MS

Comprehensive Screening of Polycyclic Aromatic Hydrocarbons and Similar Compounds Using GC–APLI–TIMS–TOFMS/GC–EI–MS

Analysis of Peptide Stereochemistry in Single Cells by Capillary Electrophoresis–Trapped Ion Mobility Spectrometry Mass Spectrometry

Native mass spectrometry—A valuable tool in structural biology

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