Evidence map›Paper›PMID 32959654›Full record

ArticleJournal of the American Society for Mass Spectrometry2020

Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides.

Alyssa Q Stiving, Sophie R Harvey, Benjamin J Jones, Bruno Bellina, Jeffery M Brown, Perdita E Barran, Vicki H Wysocki

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
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

13 citing papers in PubMed, 15 citations in OpenAlex.

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  3. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
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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

7 authors at 3 institutions in 2 countries.

Alyssa Q StivingDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio 43210, United States.ORCID http://orcid.org/0000-0002-9334-1212
Sophie R HarveyDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio 43210, United States.ORCID http://orcid.org/0000-0003-0763-8173
Benjamin J JonesDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio 43210, United States.ORCID http://orcid.org/0000-0002-6135-4377
Bruno BellinaMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.
Jeffery M BrownWaters Corporation, Wilmslow, SK9 4AX, United Kingdom.ORCID http://orcid.org/0000-0001-8569-7174
Perdita E BarranMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom.ORCID http://orcid.org/0000-0002-7720-586X
Vicki H WysockiDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio 43210, United States.ORCID http://orcid.org/0000-0003-0495-2538
The Ohio State University · USUniversity of Manchester · GBWaters (United Kingdom) · GB

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
NIGMS NIH HHS P41 GM128577
6 · The paper itself

Abstract

Ultraviolet photodissociation (UVPD) has emerged as a useful technique for characterizing peptide, protein, and protein complex primary and secondary structure. 193 nm UVPD, specifically, enables extensive covalent fragmentation of the peptide backbone without the requirement of a specific side chain chromophore and with no precursor charge state dependence. We have modified a commercial quadrupole-ion mobility-time-of-flight (Q-IM-TOF) mass spectrometer to include 193 nm UVPD following ion mobility. Ion mobility (IM) is a gas-phase separation technique that enables separation of ions by their size, shape, and charge, providing an orthogonal dimension of separation to mass analysis. Following instrument modifications, we characterized the performance of, and information that could be generated from, this new setup using the model peptides substance P, melittin, and insulin chain B. These experiments show extensive fragmentation across the peptide backbone and a variety of ion types as expected from 193 nm UVPD. Additionally, y-2 ions (along with complementary a+2 and b+2 ions) N-terminal to proline were observed. Combining the IM separation and mobility gating capabilities with UVPD, we demonstrate the ability to accomplish both mass- and mobility-selection of bradykinin des-Arg9 and des-Arg1 peptides followed by complete sequence characterization by UVPD. The new capabilities of this modified instrument demonstrate the utility of combining IM with UVPD because isobaric species cannot be independently selected with a traditional quadrupole alone.

Indexed as

Amino Acid SequenceIonsMass SpectrometryPeptidesPhotolysisProtein Structure, SecondaryUltraviolet RaysIonsPeptides

Identifiers

PMID32959654
PMCPMC8127984
OpenAlexW3087477861

What OpenQuestion holds

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Registered trials

None linked

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.