Evidence map›Paper›PMID 20942406›Full record

ArticleAnalytical chemistry2010

Real-time hydrogen/deuterium exchange kinetics via supercharged electrospray ionization tandem mass spectrometry.

Harry J Sterling, Evan R Williams

Abstract read
In one paragraph

Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Intrinsic site-selectivity of ubiquitin dimer formation.Protein science : a publication of the Protein Society · 2015
    Article
  15. The use of chromium(III) to supercharge peptides by protonation at low basicity sites.Journal of the American Society for Mass Spectrometry · 2015
    Article
  16. Article
  17. Soft supercharging of biomolecular ions in electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014
    Article
  18. Article
  19. Article
  20. Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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.

Harry J SterlingDepartment of Chemistry, University of California, Berkeley, California 94720-1460, United States.
Evan R Williams
University of California, Berkeley · US

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Protein Conformation and Noncovalent InteractionsR01GM064712 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2002 to 2009
$2.0M
NIGMS NIH HHS R01 GM064712NIGMS NIH HHS R01GM064712NIGMS NIH HHS T32 GM008295NIGMS NIH HHS T32GM08295
6 · The paper itself

Abstract

Amide hydrogen/deuterium exchange (HDX) rate constants of bovine ubiquitin in an ammonium acetate solution containing 1% of the electrospray ionization (ESI) "supercharging" reagent m-nitrobenzyl alcohol (m-NBA) were obtained using top-down, electron transfer dissociation (ETD) tandem mass spectrometry (MS). The supercharging reagent replaces the acid and temperature "quench" step in the conventional MS approach to HDX experiments by causing rapid protein denaturation to occur in the ESI droplet. The higher charge state ions that are produced with m-NBA are more unfolded, as measured by ion mobility, and result in higher fragmentation efficiency and higher sequence coverage with ETD. Single amino acid resolution was obtained for 44 of 72 exchangeable amide sites, and summed kinetic data were obtained for regions of the protein where adjacent fragment ions were not observed, resulting in an overall spatial resolution of 1.3 residues. Comparison of these results with previous values from NMR indicates that the supercharging reagent does not cause significant structural changes to the protein in the initial ESI solution and that scrambling or back-exchange is minimal. This new method for top-down HDX-MS enables real-time kinetic data measurements under physiological conditions, similar to those obtained using NMR, with comparable spatial resolution and significantly better sensitivity.

Indexed as

Amino Acid SequenceAnimalsCattleDeuteriumDeuterium Exchange MeasurementHydrogenKineticsMolecular Sequence DataSpectrometry, Mass, Electrospray IonizationUbiquitinDeuteriumHydrogenUbiquitin

Identifiers

PMID20942406
PMCPMC3049191
OpenAlexW2059640916

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.