Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins (pages 4508–4512)
Dr. Rasmus Linser, Muralidhar Dasari, Dr. Matthias Hiller, Dr. Victoria Higman, Uwe Fink, Dr. Juan-Miguel Lopez del Amo, Stefan Markovic, Liselotte Handel, Brigitte Kessler, Dr. Peter Schmieder, Prof. Dr. Dieter Oesterhelt, Prof. Dr. Hartmut Oschkinat and Prof. Dr. Bernd Reif
Version of Record online: 14 APR 2011 | DOI: 10.1002/anie.201008244
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.