title: Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy.
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.
authors.affiliation: Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C, Denmark.
authors.forename: Jakob T
authors.initials: JT
authors.lastname: Nielsen
authors.forename: Morten
authors.initials: M
authors.lastname: Bjerring
authors.forename: Martin D
authors.initials: MD
authors.lastname: Jeppesen
authors.forename: Ronnie O
authors.initials: RO
authors.lastname: Pedersen
authors.forename: Jan M
authors.initials: JM
authors.lastname: Pedersen
authors.forename: Kim L
authors.initials: KL
authors.lastname: Hein
authors.forename: Thomas
authors.initials: T
authors.lastname: Vosegaard
authors.forename: Troels
authors.initials: T
authors.lastname: Skrydstrup
authors.forename: Daniel E
authors.initials: DE
authors.lastname: Otzen
authors.forename: Niels C
authors.initials: NC
authors.lastname: Nielsen
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D006801:Humans; D058228:Islet Amyloid Polypeptide; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017434:Protein Structure, Tertiary
chemical_list: D000682:Amyloid; D058228:Islet Amyloid Polypeptide