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  Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins.

Linser, R., Dasari, M., Hiller, M., Higman, V., Fink, U., Lopez del Amo, J. M., et al. (2011). Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins. Angewandte Chemie International Edition, 50(19), 4508-4512. doi:10.1002/anie.201008244.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0018-E8B4-1 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-C61B-B
Genre: Journal Article

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 Creators:
Linser, R.1, Author           
Dasari, M., Author
Hiller, M., Author
Higman, V., Author
Fink, U., Author
Lopez del Amo, J. M., Author
Markovic, S., Author
Handel, L., Author
Kessler, B., Author
Schmieder, P., Author
Oesterhelt, D., Author
Oschkinat, H., Author
Reif, B., Author
Affiliations:
1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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Free keywords: amyloid fibrils; lipid membrane; membrane proteins; outer membrane protein G; solid-state NMR spectroscopy
 Abstract: Structural characterization of insoluble proteins often relies on solid-state NMR spectroscopy. Perdeuteration and partial back-substitution of exchangeable protons, as proposed for crystalline model proteins, is now shown to lead to beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimer's disease β-amyloid peptide Aβ40, the lipid reconstituted β-barrel membrane protein OmpG, and the α-helical membrane protein bacteriorhodopsin.

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Language(s): eng - English
 Dates: 2011-04-202011-05-02
 Publication Status: Issued
 Pages: -
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 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201008244
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Title: Angewandte Chemie International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 50 (19) Sequence Number: - Start / End Page: 4508 - 4512 Identifier: -