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.
- Markovic, S.
- Handel, L.
- Kessler, B.
- Schmieder, P.
- Oesterhelt, D.
- Oschkinat, H.
- Reif, B.
DOIAbstract
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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