Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins
R. Linser; M. Dasari; M. Hiller; V. Higman; U. Fink; J.M. Lopez Del Amo; S. Markovic; L. Handel; B. Kessler; P. Schmieder; D. Oesterhelt; H. Oschkinat*; B. Reif*
Angew. Chem. Int. Ed. 50, 4508-4512 (2011)
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 yield beneficial proton spectra for heterogeneous systems, such as fibrils formed by the Alzheimers disease b-amyloid peptide Ab40, the lipid reconstituted b-barrel membrane protein OmpG, and the ahelical membrane protein bacteriorhodopsin.
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