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Keywords:

  • amyloid fibrils;
  • NMR spectroscopy;
  • peptides;
  • supramolecular chemistry

Abstract

Thumbnail image of graphical abstract

The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 Å 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.