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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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 Creators:
Urner, Leonhard H.1, Author
Liko, Idlir2, 3, Author
Yen, Hsin-Yung2, 3, Author
Hoi, Kin-Kuan2, Author
Bolla, Jani Reddy2, Author
Gault, Joseph2, Author
Almeida, Fernando Gonçalves3, Author
Schweder, Marc-Philip1, Author
Shutin, Denis2, Author
Ehrmann, Svenja1, Author
Haag, Rainer1, Author
Robinson, Carol V.2, Author
Pagel, Kevin1, 4, Author                 
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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 Abstract: 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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Language(s): eng - English
 Dates: 2019-06-182019-12-192020-01-282020-01
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-14424-8
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: 10 Volume / Issue: 11 (1) Sequence Number: 564 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723