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Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings

Bibow, Stefan and Carneiro, Marta G. and Sabo, T. Michael and Schwiegk, Claudia and Becker, Stefan and Riek, Roland and Lee, Donghan. (2014) Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings. Protein Science, 23 (7). pp. 851-856.

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Official URL: https://edoc.unibas.ch/93834/

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Abstract

Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be obtained by measuring residual dipolar couplings (RDCs) with the outer membrane protein OmpX embedded in nanodiscs using Pf1 phage as an alignment medium. The presented collection of membrane protein RDCs in nanodiscs represents an important step toward more comprehensive structural and dynamical NMR-based investigations of membrane proteins in a natural bilayer environment.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Bibow, Stefan
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Cambridge University Press
ISSN:0961-8368
e-ISSN:1469-896X
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:07 Mar 2023 11:18
Deposited On:07 Mar 2023 11:18

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