Evidence map›Paper›PMID 26596460›Full record

ArticleThe Analyst2016

Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry.

Lindsay J Morrison, Jennifer S Brodbelt

Open access · greenAbstract read
In one paragraph

Article in The Analyst, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 66 citations in OpenAlex.

  1. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  2. Article
  3. Article
  4. Direct Identification of Intact Proteins Using a Low-Resolution Mass Spectrometer with CIDJournal of the American Society for Mass Spectrometry · 2024
    Article
  5. Article
  6. Article
  7. Article
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  12. Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Top-Down Analysis of Proteins in Low Charge States.Journal of the American Society for Mass Spectrometry · 2019
    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 at 1 institution in 1 country.

Lindsay J MorrisonDepartment of Chemistry, University of Texas, Austin, TX 78712, USA. jbrodbelt@cm.utexas.edu.
Jennifer S Brodbelt
The University of Texas at Austin · US

Funding

IRACDA Postdoctoral Program: Collaborative Opportunities for Research EducatorsK12GM102745 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2013 to 2017
$2.2M
NIGMS NIH HHS 1K12GM102745NIGMS NIH HHS K12 GM102745
6 · The paper itself

Abstract

Characterization of all gas-phase charge sites of natively sprayed proteins and peptides is demonstrated using 193 nm UVPD. The high sequence coverage offered by UVPD is exploited for the accurate determination of charge sites in protein systems up to 18 kDa, allowing charge site to be studied as a function of protein conformation and the presence of disulfide bonds. Charging protons are found on both basic sidechains and on the amide backbone of less basic amino acids such as serine, glutamine, and proline. UVPD analysis was performed on the 3+ charge state of melittin, the 5+ to 8+ charge states of ubiquitin, and the 8+ charge state of reduced and oxidized β-lactoglobulin. The location of charges in gas-phase proteins is known to impact structure; molecular modeling of different charge site motifs of 3+ melittin demonstrates how placement of protons in simulations can dramatically impact the predicted structure of the molecule. The location of positive charge sites in ubiquitin and β-lactoglobulin are additionally found to depend on the presence or absence of salt-bridges, columbic repulsion across the length of the peptide, and protein conformation. Charge site isomers are demonstrated for ubiquitin and β-lactoglobulin but found to be much less numerous than previously predicted.

Indexed as

PhotolysisUltraviolet RaysAmino Acid SequenceMass SpectrometryModels, MolecularProtein ConformationProteinsProteins

Identifiers

PMID26596460
PMCPMC4679510
OpenAlexW2174392265

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.