Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins

Angewandte Chemie, 2011, DOI: 10.1002/anie.201008244, Volume 50, Issue 19, pages 4508–4512 published on 02.05.2011

Angewandte Chemie, online article

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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