Amyloid
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Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure and ability to be stained by particular dyes, such as Congo
Micrograph showing amyloid deposits (pink) in small bowel. Duodenum with amyloid deposition in lamina propria. Amyloid shows up as homogeneous pink material in lamina propria and around blood vessels. 20× magnification.
Amyloid of HET-s(218–289) prion pentamer, Podospora anserina (PDB: 2rnm)
Structure of a fibril, consisting of one single protofilament, of the amyloid β peptide viewed down the long axis of the fibril (PDB: 2mlq)
Mechanisms of amyloid fibril formation including nucleated polymerisation (red arrows), nucleated conformational conversion (blue arrows), native-like aggregation (green arrows) and secondary processes (right)
Protein folding
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Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional s
Amyloid
…the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells. These protein misfolding and deposition processes disrupt the healthy function of tissues and organs…
All forms of protein structure summarized
Example of a small eukaryotic heat shock protein