Evidence map›Paper›PMID 22298288›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Polar aprotic modifiers for chromatographic separation and back-exchange reduction for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry.

Santosh G Valeja, Mark R Emmett, Alan G Marshall

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Review
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  14. Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment.Journal of the American Society for Mass Spectrometry · 2012
    Article
  15. 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

3 authors.

Santosh G ValejaDepartment of Chemistry and Biochemistry, 95 Chieftain Way, Florida State University, Tallahassee, FL 32306, USA.
Mark R Emmett
Alan G Marshall

Funding

Structural Mapping of Protein Complexes by Hydrogen/Deuterium ExchangeR01GM078359 · NIGMS · FLORIDA STATE UNIVERSITY · PI MARSHALL, ALAN G · 2006 to 2009
$1.2M
NIGMS NIH HHS R01 GM078359NIGMS NIH HHS R01 GM78359
6 · The paper itself

Abstract

Hydrogen/deuterium exchange monitored by mass spectrometry is an important non-perturbing tool to study protein structure and protein–protein interactions. However, water in the reversed-phase liquid chromatography mobile phase leads to back-exchange of D for H during chromatographic separation of proteolytic peptides following H/D exchange, resulting in incorrect identification of fast-exchanging hydrogens as unexchanged hydrogens. Previously, fast high-performance liquid chromatography (HPLC) and supercritical fluid chromatography have been shown to decrease back-exchange. Here, we show that replacement of up to 40% of the water in the LC mobile phase by the modifiers, dimethylformamide (DMF) and N-methylpyrrolidone (NMP) (i.e., polar organic modifiers that lack rapid exchanging hydrogens), significantly reduces back-exchange. On-line LC micro-ESI FT-ICR MS resolves overlapped proteolytic peptide isotopic distributions, allowing for quantitative determination of the extent of back-exchange. The DMF modified solvent composition also improves chromatographic separation while reducing back-exchange relative to conventional solvent.

Indexed as

AnimalsChromatography, High Pressure LiquidChromatography, Reverse-PhaseDeuterium Exchange MeasurementDimethylformamideFourier AnalysisHorsesHumansHydrophobic and Hydrophilic InteractionsMass SpectrometryPeptide FragmentsProteinsPyrrolidinonesDimethylformamideN-methylpyrrolidonePeptide FragmentsProteinsPyrrolidinones

Identifiers

PMID22298288
PMCPMC3835171

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Registered trials

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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.