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Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: Perspectives for DNP.
J. Biomol. NMR 56, 359-363 (2013)
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.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Dynamic nuclear polarization (DNP); Magic angle spinning (MAS); Solid-state; NMR high magnetic fields; Alzheimer’s β-amyloid fibrils; Dynamic-nuclear-polarization ; Spectroscopy ; Transition ; Proteins
ISSN (print) / ISBN
0925-2738
e-ISSN
1573-5001
Zeitschrift
Journal of Biomolecular NMR
Quellenangaben
Band: 56,
Heft: 4,
Seiten: 359-363
Verlag
Springer
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)