Communication

Prion Protein Amyloid Formation Involves Structural Rearrangements in the C-Terminal Domain

  1. Jitendra Kumar1,
  2. Sridhar Sreeramulu Dr.1,
  3. Thorsten L. Schmidt2,
  4. Christian Richter Dr.1,
  5. Janet Vonck Dr.3,
  6. Alexander Heckel Prof. Dr.2,
  7. Clemens Glaubitz Prof. Dr.4,
  8. Harald Schwalbe Prof. Dr.1

Article first published online: 10 MAY 2010

DOI: 10.1002/cbic.201000076

Issue

ChemBioChem

ChemBioChem

Volume 11, Issue 9, pages 1208–1213, June 14, 2010

Additional Information

How to Cite

Kumar, J., Sreeramulu, S., Schmidt, T. L., Richter, C., Vonck, J., Heckel, A., Glaubitz, C. and Schwalbe, H. (2010), Prion Protein Amyloid Formation Involves Structural Rearrangements in the C-Terminal Domain. ChemBioChem, 11: 1208–1213. doi: 10.1002/cbic.201000076

Author Information

  1. 1

    Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Organic Chemistry and Chemical Biology, Goethe University Frankfurt, Max-von-Laue-Strasse 7–9, 60438 Frankfurt/Main (Germany), Fax: (+49) 69-7982-9515

  2. 2

    Institute for Organic Chemistry and Chemical Biology, Cluster of Excellence Macromolecular Complexes, Goethe University Frankfurt, Max-von-Laue-Strasse 7–9, 60438 Frankfurt/Main (Germany)

  3. 3

    Department of Structural Biology, Max Planck Institute for Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt/Main (Germany)

  4. 4

    Center for Biomolecular Magnetic Resonance (BMRZ), Institute for Biophysical Chemistry, Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438 Frankfurt/Main (Germany)

Publication History

  1. Issue published online: 7 JUN 2010
  2. Article first published online: 10 MAY 2010
  3. Manuscript Received: 9 FEB 2010

Funded by

  • EU NMR
  • MPI graduate college (IMPRES)

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Keywords:

  • aggregation;
  • amyloid beta-peptides;
  • misfolding;
  • NMR spectroscopy;
  • prions
Thumbnail image of graphical abstract

Hard core: We have analyzed the structural rearrangements of the urea-denatured state of recombinant prion protein by using liquid-state NMR spectroscopy. Our studies document that prion amyloid fibrils generated from monomeric, urea-unfolded human prion protein have a rigid core between residues 145–223.

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