Evidence map›Paper›PMID 34109026›Full record

ArticleChemical science2020

A new azobenzene-based design strategy for detergents in membrane protein research.

Leonhard H Urner, Maiko Schulze, Yasmine B Maier, Waldemar Hoffmann, Stephan Warnke, Idlir Liko, Kristin Folmert, Christian Manz, Carol V Robinson, Rainer Haag and 1 more

Abstract read
In one paragraph

Article in Chemical science, 2020. 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
–field-weighted citation impact
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.

  1. Article
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  8. Emergence of mass spectrometry detergents for membrane proteomics.Analytical and bioanalytical chemistry · 2023
    Review
  9. Review
  10. Article
  11. Article
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  14. Review
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

11 authors.

Leonhard H UrnerInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.ORCID https://orcid.org/0000-0001-8144-8955
Maiko SchulzeInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.
Yasmine B MaierInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.
Waldemar HoffmannInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.
Stephan WarnkeDepartment of Molecular Physics, Fritz Haber Institute of the Max Planck Society Faradayweg 4-6 14195 Berlin Germany kevin.pagel@fu-berlin.de.
Idlir LikoPhysical and Theoretical Chemistry Laboratory, University of Oxford South Parks Road OX13QZ Oxford UK.
Kristin FolmertInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.
Christian ManzInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.ORCID https://orcid.org/0000-0003-2975-5450
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, University of Oxford South Parks Road OX13QZ Oxford UK.ORCID https://orcid.org/0000-0002-7958-4074
Rainer HaagInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.
Kevin PagelInstitute of Chemistry and Biochemistry, Freie Universität Berlin Arnimallee 22 14195 Berlin Germany leonhard.urner@fu-berlin.de.ORCID https://orcid.org/0000-0001-8054-4718

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mass spectrometry enables the in-depth structural elucidation of membrane protein complexes, which is of great interest in structural biology and drug discovery. Recent breakthroughs in this field revealed the need for design rules that allow fine-tuning the properties of detergents in solution and gas phase. Desirable features include protein charge reduction, because it helps to preserve native features of protein complexes during transfer from solution into the vacuum of a mass spectrometer. Addressing this challenge, we here present the first systematic gas-phase study of azobenzene detergents. The utility of gas-phase techniques for monitoring light-driven changes of isomer ratios and molecular properties are investigated in detail. This leads to the first azobenzene detergent that enables the native mass spectrometry analysis of membrane proteins and whose charge-reducing properties can be tuned by irradiation with light. More broadly, the presented work outlines new avenues for the high-throughput characterization of supramolecular systems and opens a new design strategy for detergents in membrane protein research.

Identifiers

PMID34109026
PMCPMC8152689

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Registered trials

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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.