Evidence map›Paper›PMID 27340830›Full record

ArticleAnalytical chemistry2016

Oversampling Selective Accumulation Trapped Ion Mobility Spectrometry Coupled to FT-ICR MS: Fundamentals and Applications.

Paolo Benigni, Francisco Fernandez-Lima

Abstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Article
  2. Linker H1 Histone Direct Top-Down Proteoform Analysis.Journal of proteome research · 2025
    Article
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  8. Towards Discovery and Targeted Peptide Biomarker Detection Using nanoESI-TIMS-TOF MS.Journal of the American Society for Mass Spectrometry · 2018
    Article
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  16. Structures of the kinetically trapped i-motif DNA intermediates.Physical chemistry chemical physics : PCCP · 2016
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Paolo BenigniDepartment of Chemistry and Biochemistry and ‡Biomolecular Sciences Institute, Florida International University , Miami, Florida 33199, United States.
Francisco Fernandez-LimaDepartment of Chemistry and Biochemistry and ‡Biomolecular Sciences Institute, Florida International University , Miami, Florida 33199, United States.

Funding

Mass Spectrometry based molecular imaging of native biological nanodomainsR00GM106414 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI FERNANDEZ-LIMA, FRANCISCO · 2012 to 2014
$731k
NIGMS NIH HHS R00 GM106414
6 · The paper itself

Abstract

In the present paper, we describe the fundamentals and analytical advantages of Oversampling Selective Accumulation Trapped Ion Mobility Spectrometry (OSA-TIMS) when coupled to ultrahigh resolution mass analyzers (e.g., FT-ICR MS). During TIMS analysis, ion packages are spatially resolved based on their mobilities along the TIMS analyzer axis and multiple strategies can be utilized during the trapping and elution of the ion population of interest. In the case of OSA-TIMS-FT-ICR MS, the TIMS operation sequence, trapping conditions, and operations are optimized to increase the signal-to-noise and the number of points across the mobility domain, which leads to more accurate mobility and mass measurements. Experimental results show that accurate ion-neutral collision cross sections (<1%) can be measured using OSA-TIMS-FT-ICR MS with high mobility resolving powers (RIMS up to 250), high mass accuracy (<1 ppm), and ultrahigh mass resolution (RMS up to 600-1200k at m/z 400) in a single analysis. The analytical advantages of OSA-TIMS over SA-TIMS were illustrated for the analysis of structural peptide isomers (SDGRG and GRGDS [M + H](+)), conformational isomers (AT-hook peptide 3 KRGRGRPRK [M + 2H](+2)), and a complex mixture of polyaromatic hydrocarbons (PAH) from coal tar. Baseline separation of the structural peptide isomers SDGRG and GRGDS, [M + H](+), was observed, and three conformations were identified for the AT-hook peptide 3 KRGRGRPRK [M + 2H](+2) during OSA-TIMS-FT-ICR MS. A 2-fold increase in the number of molecular features and a 2-6-fold signal-to-noise increase was observed for OSA-TIMS when compared with SA-TIMS during the PAH analysis. This work provides the proof-of-principle for further application of OSA-TIMS-FT-ICR MS for the unsupervised analysis of complex mixtures based on the characterization of the conformational space and the assignment of chemical formulas in a single analysis.

Indexed as

Ion Mobility SpectrometrySpectrometry, Mass, Electrospray IonizationAmino Acid SequenceCoal TarFourier AnalysisIsomerismNanotechnologyPeptidesPolycyclic Aromatic HydrocarbonsCoal TarPeptidesPolycyclic Aromatic Hydrocarbons

Identifiers

PMID27340830
PMCPMC13587742

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.