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

被引：32

作者：

Lopez del Amo, Juan-Miguel ^{[1
,2
,3
]}

Schneider, Dennis ^{[4
]}

Loquet, Antoine ^{[5
]}

Lange, Adam ^{[5
]}

Reif, Bernd ^{[1
,2
,3
]}

机构：

[1] Deutsch Forschungszentrum Gesundheit & Umwelt, Helmholtz Zentrum Munchen HMGU, D-85764 Neuherberg, Germany

[2] TUM, Dept Chem, Munich Ctr Integrated Prot Sci CIPS M, D-85747 Garching, Germany

[3] Leibniz Inst Mol Pharmakol FMP, D-13125 Berlin, Germany

[4] Bruker BioSpin, D-76287 Im Siberstreifen, Rheinstetten, Germany

[5] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

来源：

JOURNAL OF BIOMOLECULAR NMR | 2013年 / 56卷 / 04期

关键词：

Dynamic nuclear polarization (DNP); Magic angle spinning (MAS); Solid-state; NMR high magnetic fields; Alzheimer's beta-amyloid fibrils; DYNAMIC-NUCLEAR-POLARIZATION; TRANSITION;

D O I：

10.1007/s10858-013-9755-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 beta-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.

引用

页码：359 / 363

页数：5

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