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Journal Article

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

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Linser,  R.
Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society;

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2000135_Suppl.pdf
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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0018-E8B4-1
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.