Evidence map›Paper›PMID 30885379›Full record

ArticleBiophysical journal2019

Estimating Constraints for Protection Factors from HDX-MS Data.

Simon P Skinner, Gael Radou, Roman Tuma, Jeanine J Houwing-Duistermaat, Emanuele Paci

Abstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. HXMS: a standardized file format for HX-MS data.Bioinformatics (Oxford, England) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Fundamentals of HDX-MS.Essays in biochemistry · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. 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

5 authors.

Simon P SkinnerAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Cellular and Molecular Biology, University of Leeds, Leeds, United Kingdom.
Gael RadouAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Cellular and Molecular Biology, University of Leeds, Leeds, United Kingdom.
Roman TumaAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Cellular and Molecular Biology, University of Leeds, Leeds, United Kingdom; Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
Jeanine J Houwing-DuistermaatSchool of Mathematics, University of Leeds, Leeds, United Kingdom; Department of Biostatistics and Research Support, Julius Center, UMC Utrecht, The Netherlands.
Emanuele PaciAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Cellular and Molecular Biology, University of Leeds, Leeds, United Kingdom. Electronic address: e.paci@leeds.ac.uk.

Funding

Wellcome TrustWellcome Trust 096686/Z/11/Z
6 · The paper itself

Abstract

Hydrogen/deuterium exchange monitored by mass spectrometry is a promising technique for rapidly fingerprinting structural and dynamical properties of proteins. The time-dependent change in the mass of any fragment of the polypeptide chain depends uniquely on the rate of exchange of its amide hydrogens, but determining the latter from the former is generally not possible. Here, we show that, if time-resolved measurements are available for a number of overlapping peptides that cover the whole sequence, rate constants for each amide hydrogen exchange (or equivalently, their protection factors) may be extracted and the uniqueness of the solutions obtained depending on the degree of peptide overlap. However, in most cases, the solution is not unique, and multiple alternatives must be considered. We provide a statistical method that clusters the solutions to further reduce their number. Such analysis always provides meaningful constraints on protection factors and can be used in situations in which obtaining more refined experimental data is impractical. It also provides a systematic way to improve data collection strategies to obtain unambiguous information at single-residue level (e.g., for assessing protein structure predictions at atomistic level).

Indexed as

AmidesComplement C3DeuteriumHydrogen BondingMass SpectrometryPeptidesAmidesComplement C3DeuteriumPeptides

Identifiers

PMID30885379
PMCPMC6451051

What OpenQuestion holds

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LicenceCC BY
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.