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  Probing membrane protein insertion into lipid bilayers by solid-state NMR.

Najbauer, E., Movellan, K. T., Schubeis, T., Schwarzer, T., Castiglione, K., Giller, K., et al. (2019). Probing membrane protein insertion into lipid bilayers by solid-state NMR. ChemPhysChem, 20(2), 302-310. doi:10.1002/cphc.201800793.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-84FD-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-D61A-0
Genre: Journal Article

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 Creators:
Najbauer, E.1, Author              
Movellan, K. T., Author
Schubeis, T., Author
Schwarzer, T., Author
Castiglione, K., Author
Giller, K.1, Author              
Pintacuda, G., Author
Becker, S.1, Author              
Andreas, L.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
2Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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Free keywords: Lipid bilayer; magic-angle spinning; membrane protein; solid state NMR; surface environment
 Abstract: Determination of the environment surrounding a protein is often key to understanding function, and can also be used to infer structural properties of the protein itself. Using proton-detected solid-state NMR, we show that reduced spin diffusion within the protein under conditions of fast magic-angle spinning, high magnetic field, and sample deuteration allows the efficient measurement of site-specific exposure to mobile water and lipids. We demonstrate this site specificity on two membrane proteins, the human voltage dependent anion channel, and the alkane transporter AlkL from Pseudomonas putida. Transfer from lipids is observed selectively in the membrane spanning region, and an average lipid-protein transfer rate of 6 s¯¹ was determined for residues protected from exchange. Transfer within the protein, as tracked in the ¹⁵N-¹H 2D plane, was estimated from initial rates and found to be in a similar range of about 8 to 15 s-1 for several resolved residues, explaining the site specificity.

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Language(s): eng - English
 Dates: 2018-11-192019-01-21
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/cphc.201800793
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Title: ChemPhysChem
Source Genre: Journal
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Pages: - Volume / Issue: 20 (2) Sequence Number: - Start / End Page: 302 - 310 Identifier: -