Evidence map›Paper›PMID 24410546›Full record

ArticleAnalytical chemistry2014

Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.

Catherine A Cassou, Evan R Williams

Open access · bronzeAbstract read
In one paragraph

Article in Analytical chemistry, 2014. 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
4.4field-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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. The Role of Nanobubbles in Protein Unfolding during Electrothermal Supercharging.Journal of the American Society for Mass Spectrometry · 2025
    Article
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  8. Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips.Journal of the American Society for Mass Spectrometry · 2017
    Article
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  13. Article
  14. The use of chromium(III) to supercharge peptides by protonation at low basicity sites.Journal of the American Society for Mass Spectrometry · 2015
    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.

Catherine A CassouDepartment of Chemistry, University of California , Berkeley, California 94720-1460, United States.
Evan R Williams
University of California, Berkeley · US

Funding

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
Integrated Methods for Structural Elucidation of Proteins and Macromolecular CompR01GM097357 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2012 to 2015
$1.0M
NIGMS NIH HHS R01 GM096097NIGMS NIH HHS R01 GM097357NIGMS NIH HHS R01GM097357
6 · The paper itself

Abstract

The effects of different anions on the extent of electrothermal supercharging of proteins from aqueous ammonium and sodium salt solutions were investigated. Sulfate and hydrogen phosphate are the most effective anions at producing high charge state protein ions from buffered aqueous solution, whereas iodide and perchlorate are ineffective with electrothermal supercharging. The propensity for these anions to produce high charge state protein ions follows the following trend: sulfate > hydrogen phosphate > thiocyanate > bicarbonate > chloride > formate ≈ bromide > acetate > iodide > perchlorate. This trend correlates with the reverse Hofmeister series over a wide range of salt concentrations (1 mM to 2 M) and with several physical properties, including solvent surface tension, anion viscosity B-coefficient, and anion surface/bulk partitioning coefficient, all of which are related to the Hofmeister series. The effectiveness of electrothermal supercharging does not depend on bubble formation, either from thermal degradation of the buffer or from coalescence of dissolved gas. These results provide evidence that the effect of different ions in the formation of high charge state ions by electrothermal supercharging is largely a result of Hofmeister effects on protein stability leading to protein unfolding in the heated ESI droplet.

Indexed as

TemperatureAmmonium CompoundsAnimalsCattleProteinsProtein StabilityProtein UnfoldingSaltsSodiumSpectrometry, Mass, Electrospray IonizationWaterAmmonium CompoundsProteinsSaltsSodiumWater

Identifiers

PMID24410546
PMCPMC3983018
OpenAlexW2325863054

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.