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Updated: Jul 4, 2026

05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Polymorphism in an amyloid-like fibril-forming model peptide
René Verel1, Ivan T Tomka, Carlo Bertozzi
1Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
Angewandte Chemie (International Ed. in English)
|June 6, 2008
Summary
No abstract available in PubMed .
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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