Evidence map›Paper›PMID 32005983›Full record

ArticleNature protocols2020

Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry.

Zachary L VanAernum, Florian Busch, Benjamin J Jones, Mengxuan Jia, Zibo Chen, Scott E Boyken, Aniruddha Sahasrabuddhe, David Baker, Vicki H Wysocki

Open access · greenAbstract read
In one paragraph

Article in Nature protocols, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 166 citations in OpenAlex.

  1. Review
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  9. From inflammation to remodelling: A novel BASP1Journal of advanced research · 2025
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24 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 1 country.

Zachary L VanAernum *Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.ORCID http://orcid.org/0000-0002-0956-3956
Florian Busch *Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Benjamin J JonesDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.ORCID http://orcid.org/0000-0002-6135-4377
Mengxuan JiaDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Zibo ChenDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-2990-2895
Scott E BoykenDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Aniruddha SahasrabuddheDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA. wysocki.11@osu.edu.ORCID http://orcid.org/0000-0003-0495-2538
The Ohio State University · USAmgen (United States) · USCalifornia Institute of Technology · USHoward Hughes Medical Institute · USUniversity of Washington · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI SOMOGYI, ARPAD · 2018 to 2022
$7.6M
15 Tesla Bruker solariX FTICR MSS10OD018507 · OD · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2014 to 2014
$2.0M
NIGMS NIH HHS P41 GM128577NIH HHS S10 OD018507ODCDC CDC HHS S10 OD018507
6 · The paper itself

Abstract

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is time-consuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes or clarified cell lysates. In the liquid chromatography coupled to mass spectrometry (LC-MS) approach described in this protocol, samples in MS-incompatible conditions are injected onto a short size-exclusion chromatography column. Proteins and protein complexes are separated from small molecule non-volatile buffer components using an aqueous, non-denaturing mobile phase. Eluted proteins and protein complexes are detected by the mass spectrometer after electrospray ionization. Mass spectra can inform regarding protein sample purity and oligomerization, and additional tandem mass spectra can help to further obtain information on protein complex subunits. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization.

Indexed as

BuffersChemistry Techniques, AnalyticalChromatography, GelMass SpectrometryProteinsBuffersProteins

Identifiers

PMID32005983
PMCPMC7203678
OpenAlexW3004074111

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.