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  Proton-based structural analysis of a heptahelical transmembrane protein in lipid bilayers.

Lalli, D., Idso, M. N., Andreas, L. B., Hussain, S., Baxter, N., Han, S., et al. (2017). Proton-based structural analysis of a heptahelical transmembrane protein in lipid bilayers. Journal of the American Chemical Society, 139(37), 13006-13012. doi:10.1021/jacs.7b05269.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2ED9-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-2EDE-3
Genre: Journal Article

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Lalli, D., Author
Idso, M. N., Author
Andreas, L. B.1, Author              
Hussain, S., Author
Baxter, N., Author
Han, S., Author
Chmelka, B. F., Author
Pintacuda, G., Author
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1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              

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 Abstract: The structures and properties of membrane proteins in lipid bilayers are expected to closely resemble those in native cell-membrane environments, although they have been difficult to elucidate. By performing solid-state NMR measurements at very fast (100 kHz) magic-angle spinning rates and at high (23.5 T) magnetic field, severe sensitivity and resolution challenges are overcome, enabling the atomic-level characterization of membrane proteins in lipid environments. This is demonstrated by extensive 1H-based resonance assignments of the fully protonated heptahelical membrane protein proteorhodopsin, and the efficient identification of numerous 1H–1H dipolar interactions, which provide distance constraints, inter-residue proximities, relative orientations of secondary structural elements, and protein–cofactor interactions in the hydrophobic transmembrane regions. These results establish a general approach for high-resolution structural studies of membrane proteins in lipid environments via solid-state NMR.

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Language(s): eng - English
 Dates: 2017-07-202017-09-20
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.7b05269
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 139 (37) Sequence Number: - Start / End Page: 13006 - 13012 Identifier: -