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Updated: Jun 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
[Structure of amyloid fibrils]
1Leibniz-Institut für Altersforschung (Fritz-Lipmann-Institut), Jena, Deutschland.
Abstract:
Amyloid fibrils are structurally defined as fibrillar polypeptide aggregates with a characteristic cross-beta structure. Such fibrils can be formed by certain polypeptide sequences in the human body and by numerous polypeptide sequences in vitro. All amyloid fibrils possess a structural spine that is formed by a cross-beta structure. This structure is stabilized by hydrogen bonds between the polypeptide backbone. In recent years, various biophysical techniques, such as X-ray crystallography, solid state nuclear magnetic resonance spectroscopy and electron cryo-microscopy have provided insights into the structural organization of amyloid fibrils. This review presents an overview of important results obtained with these methods.
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