Evidence map›Paper›PMID 20712348›Full record

ArticleAnalytical chemistry2010

Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions.

Anastasia Kharlamova, Boone M Prentice, Teng-Yi Huang, Scott A McLuckey

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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Single-Frequency Ion Parking in a Digital 3D Quadrupole Ion Trap.International journal of mass spectrometry · 2024
    Article
  7. Article
  8. Article
  9. Light-coupled cryo-plunger for time-resolved cryo-EM.Journal of structural biology · 2020
    Article
  10. Electrospray Photochemical Oxidation of Proteins.Journal of the American Society for Mass Spectrometry · 2019
    Article
  11. Article
  12. Article
  13. Joule Heating and Thermal Denaturation of Proteins in Nano-ESI Theta Tips.Journal of the American Society for Mass Spectrometry · 2017
    Article
  14. Article
  15. Article
  16. Charging of Proteins in Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017
    Article
  17. Article
  18. Article
  19. Increasing protein charge state when using laser electrospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 2015
    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

4 authors at 1 institution in 1 country.

Anastasia KharlamovaDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907-2084, USA.
Boone M Prentice
Teng-Yi Huang
Scott A McLuckey
Purdue University West Lafayette · US

Funding

Gas-phase Bio-conjugation in the Tandem Mass Spectrometry of Peptides, Proteins,R37GM045372 · NIGMS · PURDUE UNIVERSITY · PI MCLUCKEY, SCOTT A · 2014 to 2023
$3.1M
INSTRUMENTATION FOR ANALYSIS OF HIGH MASS BIOMOLECULESR01GM045372 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI MCLUCKEY, SCOTT A · 1991 to 2012
$2.8M
NIGMS NIH HHS GM 45372NIGMS NIH HHS R01 GM045372NIGMS NIH HHS R37 GM045372
6 · The paper itself

Abstract

The exposure of electrospray droplets to acid vapors can significantly affect protein charge state distributions (CSDs) derived from unbuffered solutions. Such experiments have been conducted by leaking acidic vapors into the counter-current nitrogen drying gas of an electrospray interface. On the basis of changes in protein CSDs, protein folding and unfolding phenomena are implicated in these studies. Additionally, noncovalently bound complexes are preserved, and transient intermediates are observed, such as high charge state ions of holomyoglobin. CSDs of proteins containing disulfide bonds shift slightly, if at all, with acid vapor leak-in, but when these disulfide bonds are reduced in solution, charge states higher than the number of basic sites (Lys, Arg, His, and N-terminus) are observed. Since there is no observed change in the CSD of buffered proteins exposed to acidic vapors, this novel multiple charging phenomenon is attributed to a pH effect. Thus, this acid vapor leak-in approach can be used to reverse "wrong-way-round" nanoelectrospray conditions by altering solution pH in the charged droplets relative to the pH in bulk solution. In general, the exposure of electrospray droplets to acidic vapors provides means for altering protein CSDs independent of bulk unbuffered solution pH.

Indexed as

Cytochromes cGasesHydrogen-Ion ConcentrationMyoglobinProtein ConformationProtein FoldingProteinsSolventsTandem Mass SpectrometryCytochromes cGasesMyoglobinProteinsSolvents

Identifiers

PMID20712348
PMCPMC2940272
OpenAlexW2022894679

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.