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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

Die Fibrillenstruktur, die das amyloidogene Fragment SNNFGAILSS des menschlichen Insel-Amyloid-Polypeptids (hIAPP) bildet, wurde mit einer Auflösung von 0.52 Å bestimmt. Aus den Festkörper-NMR-Spektren einfach erhältliche Symmetrieinformationen (siehe Bild) können zusammen mit langreichweitigen Randbedingungen genutzt werden, um die supramolekulare Organisation von Fibrillen eindeutig zu identifizieren.

original image

Ancillary