1. [Structure of amyloid fibrils].
- Author
-
Meinhardt J and Fändrich M
- Subjects
- Alzheimer Disease pathology, Amyloid ultrastructure, Cryoelectron Microscopy, Crystallography, X-Ray, Humans, Magnetic Resonance Spectroscopy, Neurodegenerative Diseases pathology, Peptides analysis, Prion Diseases pathology, Protein Folding, Amyloid analysis, Amyloidosis pathology
- 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.
- Published
- 2009
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