Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease 
amyloid-β peptide: perspectives for DNP.

Lopez del Amo, J. M.; Schneider, D.; Loquet, A.; Lange, A.; Reif, B.

doi:10.1007/s10858-013-9755-5

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Journal Article

Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-β peptide: perspectives for DNP.

MPS-Authors

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Loquet, A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Lange, A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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1838046_Supplement_1.docx
(Supplementary material), 786KB

Citation

Lopez del Amo, J. M., Schneider, D., Loquet, A., Lange, A., & Reif, B. (2013). Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-β peptide: perspectives for DNP. Journal of Biomolecular NMR, 56(4), 359-363. doi:10.1007/s10858-013-9755-5.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-5EBA-D

Abstract

Dynamic Nuclear Polarization solid-state NMR holds the potential to enable a dramatic increase in sensitivity by exploiting the large magnetic moment of the electron. However, applications to biological solids are hampered in uniformly isotopically enriched biomacromolecules due to line broadening which yields a limited spectral resolution at cryogenic temperatures. We show here that high magnetic fields allow to overcome the broadening of resonance lines often experienced at liquid nitrogen temperatures. For a fibril sample of the Alzheimer’s disease β-amyloid peptide, we find similar line widths at low temperature and at room temperature. The presented results open new perspectives for structural investigations in the solid-state.