dc.contributor.author
Urner, Leonhard H.
dc.contributor.author
Liko, Idlir
dc.contributor.author
Yen, Hsin-Yung
dc.contributor.author
Hoi, Kin-Kuan
dc.contributor.author
Bolla, Jani Reddy
dc.contributor.author
Gault, Joseph
dc.contributor.author
Schweder, Marc-Philip
dc.contributor.author
Ehrmann, Svenja
dc.contributor.author
Haag, Rainer
dc.contributor.author
Pagel, Kevin
dc.date.accessioned
2020-11-02T12:45:47Z
dc.date.available
2020-11-02T12:45:47Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/28740
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-28488
dc.description.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.
en
dc.format.extent
10 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
dendritic amphiphiles
en
dc.subject
mass-spectrometry
en
dc.subject
lipid-binding
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
Modular detergents tailor the purification and structural analysis of membrane proteins including G-protein coupled receptors
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
564
dcterms.bibliographicCitation.doi
10.1038/s41467-020-14424-8
dcterms.bibliographicCitation.journaltitle
Nature Communications
dcterms.bibliographicCitation.number
1
dcterms.bibliographicCitation.volume
11
dcterms.bibliographicCitation.url
https://doi.org/10.1038/s41467-020-14424-8
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2041-1723
refubium.resourceType.provider
WoS-Alert