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

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Pagel,  Kevin       
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0005-B620-9
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.