Evidence map›Paper›PMID 18461930›Full record

ArticleJournal of the American Chemical Society2008

Charge carrier field emission determines the number of charges on native state proteins in electrospray ionization.

Christopher J Hogan, James A Carroll, Henry W Rohrs, Pratim Biswas, Michael L Gross

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Strengths and Weaknesses of Molecular Simulations of Electrosprayed Droplets.Journal of the American Society for Mass Spectrometry · 2018
    Article
  10. Charging and Release Mechanisms of Flexible Macromolecules in Droplets.Journal of the American Society for Mass Spectrometry · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Do charge state signatures guarantee protein conformations?Journal of the American Society for Mass Spectrometry · 2012
    Article
  16. Supercharging protein complexes from aqueous solution disrupts their native conformations.Journal of the American Society for Mass Spectrometry · 2012
    Article
  17. Principles of electrospray ionization.Molecular & cellular proteomics : MCP · 2011
    Review
  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

5 authors.

Christopher J HoganDepartment of Energy, Environmental, & Chemical Engineering, Washington University, St. Louis, Missouri 63130, USA. cjhogan@wustl.edu
James A Carroll
Henry W Rohrs
Pratim Biswas
Michael L Gross

Funding

YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
NCRR NIH HHS P41 RR000954NCRR NIH HHS P41RR000954NIGMS NIH HHS P41 GM103422
6 · The paper itself

Abstract

Although multiple charging in electrospray ionization (ESI) is essential to protein mass spectrometry, the underlying mechanism of multiple charging has not been explicated. Here, we present a new theory to describe ESI of native-state proteins and predict the number of excess charges on proteins in ESI. The theory proposes that proteins are ionized as charged residues in ESI, as they retain residual excess charges after solvent evaporation and do not desorb from charged ESI droplets. However, their charge state is not determined by the Rayleigh limit of a droplet of similar size to the protein; rather, their final charge state is determined by the electric field-induced emission of small charged solute ions and clusters from protein-containing ESI droplets. This theory predicts that the number of charges on a protein in ESI should be directly proportional to the square of the gas-phase protein diameter and to E*, the critical electric field strength at which ion emission from droplets occurs. This critical field strength is determined by the properties of the excess charge carriers (i.e., the solute) in droplets. Charge-state measurements of native-state proteins with molecular masses in the 5-76 kDa range in ammonium acetate and triethylammonium bicarbonate are in excellent agreement with theoretical predictions and strongly support the mechanism of protein ESI proposed here.

Indexed as

ProteinsSpectrometry, Mass, Electrospray IonizationProteins

Identifiers

PMID18461930
PMCPMC2638767

What OpenQuestion holds

Textmetadata
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.