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Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid‐State NMR Spectroscopy
Authors:Jakob T. Nielsen Dr.  Morten Bjerring Dr.  Martin D. Jeppesen  Ronnie O. Pedersen  Jan M. Pedersen Dr.  Kim L. Hein  Thomas Vosegaard Dr.  Troels Skrydstrup Prof.  Daniel E. Otzen Prof.  Niels C. Nielsen Prof.
Affiliation:Center for Insoluble Protein Structures (inSPIN), Interdisciplinary Nanoscience Center (iNANO), University of Aarhus, 8000 Aarhus C (Denmark), Fax: (+45)?8619‐6199
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.
image

Keywords:amyloid fibrils  NMR spectroscopy  peptides  supramolecular chemistry
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