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Solid-state NMR as a probe of amyloid fibril structure

✍ Scribed by Robert Tycko

Publisher: Elsevier Science
Year: 2000
Tongue: English
Weight: 246 KB
Volume: 4
Category: Article
ISSN: 1367-5931
DOI: 10.1016/s1367-5931(00)00123-x

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✦ Synopsis

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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