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Solid-state NMR as a probe of amyloid fibril structure.

Authors
  • Tycko, R1
  • 1 Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. [email protected]
Type
Published Article
Journal
Current Opinion in Chemical Biology
Publisher
Elsevier
Publication Date
Oct 01, 2000
Volume
4
Issue
5
Pages
500–506
Identifiers
PMID: 11006536
Source
Medline
License
Unknown

Abstract

Amyloid fibrils are intrinsically noncrystalline, insoluble, high-molecular-weight aggregates of peptides and proteins, with considerable biomedical and biophysical significance. Solid-state NMR techniques are uniquely capable of providing high-resolution, site-specific structural constraints for amyloid fibrils, at the level of specific interatomic distances and torsion angles. So far, a relatively small number of solid-state NMR studies of amyloid fibrils have been reported. These have addressed issues about the supramolecular organization of beta-sheets in the fibrils and the peptide conformation in the fibrils, and have concentrated on the beta-amyloid peptide of Alzheimer's disease. Many additional applications of solid-state NMR to amyloid fibrils from a variety of sources are anticipated in the near future, as these systems are ideally suited for the technique and are of widespread current interest.

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