Evidence map›Paper›PMID 22161509›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Supercharging protein complexes from aqueous solution disrupts their native conformations.

Harry J Sterling, Alexander F Kintzer, Geoffrey K Feld, Catherine A Cassou, Bryan A Krantz, Evan R Williams

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
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  4. To 200,000ACS central science · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Mass, mobility and MSThe Analyst · 2017
    Article
  11. Article
  12. On the preservation of non-covalent protein complexes during electrospray ionization.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The use of chromium(III) to supercharge peptides by protonation at low basicity sites.Journal of the American Society for Mass Spectrometry · 2015
    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

6 authors.

Harry J SterlingDepartment of Chemistry, University of California-Berkeley, Berkeley, CA 94720, USA.
Alexander F Kintzer
Geoffrey K Feld
Catherine A Cassou
Bryan A Krantz
Evan R Williams

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Univ of Calif Berkeley Chemistry-Biology Interface ProgramT32GM066698 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CHANG, CHRISTOPHER J., FRANCIS, MATTHEW B · 2004 to 2023
$7.5M
Physical Principles of Bacterial Toxin Translocation across MembranesR01AI077703 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI KRANTZ, BRYAN ANDREW · 2008 to 2017
$3.3M
Development of Single Particle Analyzer of Mass and Mobility (SPAMM)R01GM096097 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2011 to 2014
$1.1M
Structural Characterization of Polypeptides, Protein Complexes, OligosaccharidesS10RR029446 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WITKOWSKA, H. EWA · 2010 to 2010
$1.0M
NCRR NIH HHS 1S10RR029446-01NCRR NIH HHS S10 RR029446NIAID NIH HHS R01 AI077703NIAID NIH HHS R01-AI077703NIGMS NIH HHS R01 GM096097NIGMS NIH HHS R01GM096097NIGMS NIH HHS T32 GM008295NIGMS NIH HHS T32GM008295NIGMS NIH HHS T32 GM066698NIGMS NIH HHS T32GM066698
6 · The paper itself

Abstract

The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the "native" complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs.

Indexed as

AcetatesAntigens, BacterialBacterial ToxinsBenzyl AlcoholsConcanavalin AGasesHydrogen-Ion ConcentrationIonsModels, MolecularOsmolar ConcentrationProtein ConformationProteinsProtein SubunitsProtein UnfoldingSpectrometry, Mass, Electrospray IonizationStatic Electricity3-nitrobenzyl alcoholAcetatesammonium acetateanthrax toxinAntigens, BacterialBacterial ToxinsBenzyl AlcoholsConcanavalin AGasesIonsProteinsProtein Subunits

Identifiers

PMID22161509
PMCPMC3265691

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.