Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy

Authors

  • Jakob T. Nielsen Dr.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Morten Bjerring Dr.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Martin D. Jeppesen,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Ronnie O. Pedersen,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Jan M. Pedersen Dr.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Kim L. Hein,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Thomas Vosegaard Dr.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Troels Skrydstrup Prof.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Daniel E. Otzen Prof.,

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • Niels C. Nielsen Prof.

    1. Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45) 8619-6199
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  • We acknowledge support from the Danish National Research Foundation, the Villum-Kann Rasmussen Foundation, the Danish Center for Scientific Computing, the Danish Natural Science Research Council, and the Danish Biotechnological Instrument Centre.

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.

original image

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