Evidence map›Paper›PMID 28674401›Full record

ArticleScientific reports2017

Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model Selection.

Boer Xie, Amika Sood, Robert J Woods, Joshua S Sharp

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Dimethylthiourea as a Quencher in Hydroxyl Radical Protein Footprinting Experiments.Journal of the American Society for Mass Spectrometry · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Protein Structure Prediction with Mass Spectrometry Data.Annual review of physical chemistry · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors.

Boer XieComplex Carbohydrate Research Center, Department of Chemistry, University of Georgia, Athens, GA, 30602, USA.
Amika SoodComplex Carbohydrate Research Center, Department of Chemistry, University of Georgia, Athens, GA, 30602, USA.
Robert J WoodsComplex Carbohydrate Research Center, Department of Chemistry, University of Georgia, Athens, GA, 30602, USA.
Joshua S SharpDepartment of BioMolecular Sciences, School of Pharmacy, University of Mississippi, Oxford, MS, 38655, USA. jsharp@olemiss.edu.

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Improved Hydroxyl Radical Footprinting for Modeling Protein StructureR01GM096049 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI SHARP, JOSHUA S · 2012 to 2016
$1.4M
Continued Development and Maintenance of GLYCAM-WebR01GM100058 · NIGMS · UNIVERSITY OF GEORGIA · PI FOLEY, B. LACHELE, WOODS, ROBERT J · 2012 to 2015
$1.1M
NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM096049NIGMS NIH HHS R01 GM100058
6 · The paper itself

Abstract

We report an integrated workflow that allows mass spectrometry-based high-resolution hydroxyl radical protein footprinting (HR-HRPF) measurements to accurately measure the absolute average solvent accessible surface area (<SASA>) of amino acid side chains. This approach is based on application of multi-point HR-HRPF, electron-transfer dissociation (ETD) tandem MS (MS/MS) acquisition, measurement of effective radical doses by radical dosimetry, and proper normalization of the inherent reactivity of the amino acids. The accuracy of the resulting <SASA> measurements was tested by using well-characterized protein models. Moreover, we demonstrated the ability to use <SASA> measurements from HR-HRPF to differentiate molecular models of high accuracy (<3 Å backbone RMSD) from models of lower accuracy (>4 Å backbone RMSD). The ability of <SASA> data from HR-HRPF to differentiate molecular model quality was found to be comparable to that of <SASA> data obtained from X-ray crystal structures, indicating the accuracy and utility of HR-HRPF for evaluating the accuracy of computational models.

Indexed as

Models, MolecularProtein ConformationProtein FootprintingChromatography, LiquidHydroxyl RadicalMuramidaseProteinsStructure-Activity RelationshipTandem Mass SpectrometryHydroxyl RadicalMuramidaseProteins

Identifiers

PMID28674401
PMCPMC5495787

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.