Evidence map›Paper›PMID 27545682›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study.

Jongcheol Seo, Waldemar Hoffmann, Stephan Warnke, Michael T Bowers, Kevin Pagel, Gert von Helden

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
13.4field-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

49 citing papers in PubMed, 135 citations in OpenAlex.

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  8. Review
  9. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
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  16. Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022
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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

6 authors at 2 institutions in 2 countries.

Jongcheol SeoFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.ORCID 0000-0001-5844-4585
Waldemar HoffmannFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.ORCID 0000-0001-6757-3151
Stephan WarnkeFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.ORCID 0000-0001-7481-286X
Michael T BowersDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.
Kevin PagelFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany.ORCID 0000-0001-8054-4718
Gert von HeldenFritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, 14195, Berlin, Germany. helden@fhi-berlin.mpg.de.ORCID 0000-0001-7611-8740
Fritz Haber Institute of the Max Planck Society · DEUniversity of California, Santa Barbara · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Can the structures of small to medium-sized proteins be conserved after transfer from the solution phase to the gas phase? A large number of studies have been devoted to this topic, however the answer has not been unambiguously determined to date. A clarification of this problem is important since it would allow very sensitive native mass spectrometry techniques to be used to address problems relevant to structural biology. A combination of ion-mobility mass spectrometry with infrared spectroscopy was used to investigate the secondary and tertiary structure of proteins carefully transferred from solution to the gas phase. The two proteins investigated are myoglobin and β-lactoglobulin, which are prototypical examples of helical and β-sheet proteins, respectively. The results show that for low charge states under gentle conditions, aspects of the native secondary and tertiary structure can be conserved.

Indexed as

LactoglobulinsMass SpectrometryModels, MolecularMyoglobinProtein ConformationSolventsLactoglobulinsMyoglobinSolventsgas-phase reactionsIR spectroscopymass spectrometryprotein foldingprotein structures

Identifiers

PMID27545682
PMCPMC5113788
OpenAlexW2517160828

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.