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

Urner, L. H., Liko, I., Yen, H.-Y., Hoi, K.-K., Bolla, J. R., Gault, J., et al. (2020). Modular detergents tailor the purification and structural analysis of membrane proteins including G-protein coupled receptors. Nature Communications, 11(1): 564. doi:10.1038/s41467-020-14424-8.

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 Urheber:
Urner, Leonhard H.1, Autor
Liko, Idlir2, 3, Autor
Yen, Hsin-Yung2, 3, Autor
Hoi, Kin-Kuan2, Autor
Bolla, Jani Reddy2, Autor
Gault, Joseph2, Autor
Almeida, Fernando Gonçalves3, Autor
Schweder, Marc-Philip1, Autor
Shutin, Denis2, Autor
Ehrmann, Svenja1, Autor
Haag, Rainer1, Autor
Robinson, Carol V.2, Autor
Pagel, Kevin1, 4, Autor                 
Affiliations:
1Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195, Berlin, Germany, ou_persistent22              
2Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, OX1 3QZ, UK, ou_persistent22              
3OMass Therapeutics, The Schrödinger Building, Heatley Road, The Oxford Science Park, Oxford, OX4 4GE, UK, ou_persistent22              
4Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              

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 Zusammenfassung: Detergents enable the purification of membrane proteins and are indispensable reagents instructural biology. Even though a large variety of detergents have been developed in the lastcentury, the challenge remains to identify guidelines that allowfine-tuning of detergents forindividual applications in membrane protein research. Addressing this challenge, here weintroduce the family of oligoglycerol detergents (OGDs). Native mass spectrometry (MS)reveals that the modular OGD architecture offers the ability to control protein purificationand to preserve interactions with native membrane lipids during purification. In addition to abroad range of bacterial membrane proteins, OGDs also enable the purification and analysisof a functional G-protein coupled receptor (GPCR). Moreover, given the modular design ofthese detergents, we anticipatefine-tuning of their properties for specific applications instructural biology. Seen from a broader perspective, this represents a significant advance forthe investigation of membrane proteins and their interactions with lipids.

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Sprache(n): eng - English
 Datum: 2019-06-182019-12-192020-01-282020-01
 Publikationsstatus: Erschienen
 Seiten: 10
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1038/s41467-020-14424-8
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Titel: Nature Communications
  Kurztitel : Nat. Commun.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: 10 Band / Heft: 11 (1) Artikelnummer: 564 Start- / Endseite: - Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723