Author
Listed:
- Leonhard H. Urner
(Freie Universität Berlin
University of Oxford)
- Idlir Liko
(University of Oxford
The Schrödinger Building)
- Hsin-Yung Yen
(University of Oxford
The Schrödinger Building)
- Kin-Kuan Hoi
(University of Oxford)
- Jani Reddy Bolla
(University of Oxford)
- Joseph Gault
(University of Oxford)
- Fernando Gonçalves Almeida
(The Schrödinger Building)
- Marc-Philip Schweder
(Freie Universität Berlin)
- Denis Shutin
(University of Oxford)
- Svenja Ehrmann
(Freie Universität Berlin)
- Rainer Haag
(Freie Universität Berlin)
- Carol V. Robinson
(University of Oxford)
- Kevin Pagel
(Freie Universität Berlin
Fritz Haber Institute of the Max Planck Society)
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.
Suggested Citation
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 & Rainer Haag & Caro, 2020.
"Modular detergents tailor the purification and structural analysis of membrane proteins including G-protein coupled receptors,"
Nature Communications, Nature, vol. 11(1), pages 1-10, December.
Handle:
RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14424-8
DOI: 10.1038/s41467-020-14424-8
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