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  Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.

Bibow, S., Carneiro, M. G., Sabo, T. M., Schwiegk, C., Becker, S., RieK, R., et al. (2014). Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings. Protein Science, 23(7), 851-856. doi:10.1002/pro.2482.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-F414-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2C4A-8
Genre: Journal Article

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 Creators:
Bibow, S., Author
Carneiro, M. G.1, Author              
Sabo, T. M.1, Author              
Schwiegk, C.1, Author              
Becker, S.1, Author              
RieK, R., Author
Lee, D.1, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: alignment medium; COCAINE; membrane protein; nanodisc; NMR; Pf1 phage; residual dipolar coupling; TROSY
 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.

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Language(s): eng - English
 Dates: 2014-04-192014-07
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.2482
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 23 (7) Sequence Number: - Start / End Page: 851 - 856 Identifier: -