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