Evidence map›Paper›PMID 19140748›Full record

ArticleAnalytical chemistry2009

Noncovalent protein tetramers and pentamers with "n" charges yield monomers with n/4 and n/5 charges.

Richard L Beardsley, Christopher M Jones, Asiri S Galhena, Vicki H Wysocki

Abstract read
In one paragraph

Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022
    Review
  8. Surface-Induced Dissociation for Protein Complex Characterization.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Article
  10. Review
  11. Article
  12. Relative interfacial cleavage energetics of protein complexes revealed by surface collisions.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
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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

4 authors.

Richard L BeardsleyDepartment of Chemistry, University of Arizona, 1306 E. University Blvd., PO Box 210041, Tucson, Arizona, USA.
Christopher M Jones
Asiri S Galhena
Vicki H Wysocki

Funding

Influence of Peptide Structure on DissociationR01GM051387 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI WYSOCKI, VICKI H. · 1994 to 2010
$2.4M
Probing the Energetics of Protein Complex FragmentationF32GM075622 · NIGMS · UNIVERSITY OF ARIZONA · PI BEARDSLEY, RICHARD L · 2005 to 2007
$74k
NIGMS NIH HHS 5R0L GM-051387NIGMS NIH HHS F32 GM 75622NIGMS NIH HHS R01 GM051387
6 · The paper itself

Abstract

In recent years mass spectrometry based techniques have emerged as structural biology tools for the characterization of macromolecular, noncovalent assemblies. Many of these efforts involve preservation of intact protein complexes within the mass spectrometer, providing molecular weight measurements that allow the determination of subunit stoichiometry and real-time monitoring of protein interactions. Attempts have been made to further elucidate subunit architecture through the dissociation of subunits from the intact complex by colliding it into inert gas atoms such as argon or xenon. Unfortunately, the amount of structural information that can be derived from such strategies is limited by the nearly ubiquitous ejection of a single, unfolded subunit. Here, we present results from the gas-phase dissociation of protein-protein complexes upon collision into a surface. Dissociation of a series of tetrameric and pentameric proteins demonstrate that alternative subunit fragments, not observed through multiple collisions with gas atoms, can be generated through surface collision. Evidence is presented for the retention of individual subunit structure, and in some cases, retention of noncovalent interactions between subunits and ligands. We attribute these differences to the rapid large energy input of ion-surface collisions, which leads to the dissociation of subunits prior to the unfolding of individual monomers.

Indexed as

Protein MultimerizationArgonC-Reactive ProteinHemoglobinsHumansMass SpectrometryPrealbuminProtein DenaturationProtein FoldingProteinsProtein Structure, QuaternarySurface PropertiesArgonC-Reactive ProteinHemoglobinsPrealbuminProteins

Identifiers

PMID19140748
PMCPMC3477242

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Registered trials

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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.