Evidence map›Paper›PMID 31992701›Full record

ArticleNature communications2020

Modular detergents tailor the purification and structural analysis of membrane proteins including G-protein coupled receptors.

Leonhard H Urner, Idlir Liko, Hsin-Yung Yen, Kin-Kuan Hoi, Jani Reddy Bolla, Joseph Gault, Fernando Gonçalves Almeida, Marc-Philip Schweder, Denis Shutin, Svenja Ehrmann and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

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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

13 authors.

Leonhard H Urner *Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0001-8144-8955
Idlir Liko *Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Hsin-Yung YenPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Kin-Kuan HoiPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Jani Reddy BollaPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.ORCID http://orcid.org/0000-0003-4346-182X
Joseph GaultPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.ORCID http://orcid.org/0000-0001-7686-2983
Fernando Gonçalves AlmeidaOMass Therapeutics, The Schrödinger Building, Heatley Road, The Oxford Science Park, Oxford, OX4 4GE, UK.
Marc-Philip SchwederInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany.
Denis ShutinPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK.
Svenja EhrmannInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany.
Rainer HaagInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany. haag@zedat.fu-berlin.de.
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK. carol.robinson@chem.ox.ac.uk.ORCID http://orcid.org/0000-0001-7829-5505
Kevin PagelInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany. kevin.pagel@fu-berlin.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Detergents enable the purification of membrane proteins and are indispensable reagents in structural biology. Even though a large variety of detergents have been developed in the last century, the challenge remains to identify guidelines that allow fine-tuning of detergents for individual applications in membrane protein research. Addressing this challenge, here we introduce the family of oligoglycerol detergents (OGDs). Native mass spectrometry (MS) reveals that the modular OGD architecture offers the ability to control protein purification and to preserve interactions with native membrane lipids during purification. In addition to a broad range of bacterial membrane proteins, OGDs also enable the purification and analysis of a functional G-protein coupled receptor (GPCR). Moreover, given the modular design of these detergents, we anticipate fine-tuning of their properties for specific applications in structural biology. Seen from a broader perspective, this represents a significant advance for the investigation of membrane proteins and their interactions with lipids.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsDetergentsEscherichia coliEscherichia coli ProteinsMass SpectrometryMembrane LipidsModels, MolecularPeptide HydrolasesProtein RefoldingReceptors, G-Protein-CoupledSolubilityBacterial Outer Membrane ProteinsBacterial ProteinsDetergentsEscherichia coli ProteinsMembrane LipidsompT protein, E coliPeptide HydrolasesReceptors, G-Protein-Coupled

Identifiers

PMID31992701
PMCPMC6987200

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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.