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Angew Chem Int Ed Engl. 2009;48(12):2118-21. doi: 10.1002/anie.200804198.

Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.

Author information

1
Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C, Denmark.

Abstract

The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 A resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils.

PMID:
19130518
DOI:
10.1002/anie.200804198
[Indexed for MEDLINE]

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