Angewandte Chemie International Edition · 2009 · 206 citations · 12 references
Life SciencesBiochemistryBiophysicsBiophysical ChemistryStructural BiologySupramolecular ChemistryMacromolecular AssemblyMacromolecular StructureProtein AggregationProtein ConformationProtein StructureSupramolecular RecognitionAmyloid FibrilsAmyloid StructureAmyloidogenic Peptides
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.
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