Evidence map›Paper›PMID 27734326›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Charging of Proteins in Native Mass Spectrometry.

Anna C Susa, Zijie Xia, Henry Y H Tang, John A Tainer, Evan R Williams

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 47 citations in OpenAlex.

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  6. Single particle charge detection mass spectrometry enables molecular characterization of lipid nanoparticles and mRNA packaging.Journal of controlled release : official journal of the Controlled Release Society · 2025
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  20. Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    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 at 3 institutions in 1 country.

Anna C SusaDepartment of Chemistry, University of California, Berkeley, CA, 94720-1460, USA.
Zijie XiaDepartment of Chemistry, University of California, Berkeley, CA, 94720-1460, USA.
Henry Y H TangDepartment of Chemistry, University of California, Berkeley, CA, 94720-1460, USA.
John A TainerMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Evan R WilliamsDepartment of Chemistry, University of California, Berkeley, CA, 94720-1460, USA. erw@berkeley.edu.
University of California, Berkeley · USLawrence Berkeley National Laboratory · USThe University of Texas MD Anderson Cancer Center · US

Funding

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 GM097357
6 · The paper itself

Abstract

Factors that influence the charging of protein ions formed by electrospray ionization from aqueous solutions in which proteins have native structures and function were investigated. Protein ions ranging in molecular weight from 12.3 to 79.7 kDa and pI values from 5.4 to 9.6 were formed from different solutions and reacted with volatile bases of gas-phase basicities higher than that of ammonia in the cell of a Fourier-transform ion cyclotron resonance mass spectrometer. The charge-state distribution of cytochrome c ions formed from aqueous ammonium or potassium acetate is the same. Moreover, ions formed from these two solutions do not undergo proton transfer to 2-fluoropyridine, which is 8 kcal/mol more basic than ammonia. These results provide compelling evidence that proton transfer between ammonia and protein ions does not limit protein ion charge in native electrospray ionization. Both circular dichroism and ion mobility measurements indicate that there are differences in conformations of proteins in pure water and aqueous ammonium acetate, and these differences can account for the difference in the extent of charging and proton-transfer reactivities of protein ions formed from these solutions. The extent of proton transfer of the protein ions with higher gas-phase basicity bases trends with how closely the protein ions are charged to the value predicted by the Rayleigh limit for spherical water droplets approximately the same size as the proteins. These results indicate that droplet charge limits protein ion charge in native mass spectrometry and are consistent with these ions being formed by the charged residue mechanism. Graphical Abstract ᅟ.

Indexed as

AcetatesAmmoniaCircular DichroismCytochromes cIon Mobility SpectrometryMolecular WeightProteinsProtonsPyridinesSolutionsSpectrometry, Mass, Electrospray IonizationWater2-fluoropyridineAcetatesAmmoniaammonium acetateCytochromes cProteinsProtonsPyridinesSolutionsWaterAmmoniumApparent gas-phase basicityCharged residue mechanismChargingCharging mechanismCircular dichroismCombined charged residue-field emission modelElectrosprayElectrospray ionizationESIGas-phase basicityIon mobilityMechanismNative electrosprayNative ESINative mass specNative mass spectrometryNative MSProtein ion chargingProton transferRayleigh limitSalts

Identifiers

PMID27734326
PMCPMC5283922
OpenAlexW2530352216

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.