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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Protein Folding01:25

Protein Folding

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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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein and Protein Structure02:15

Protein and Protein Structure

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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.
A protein's shape is critical to its function. For example, an enzyme...
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Protein Organization01:13

Protein Organization

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Updated: Jul 26, 2025

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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Amyloids and protein aggregation.

Sara Linse1, Tuomas Knowles2

  • 1Lund University, Biochemistry & Structural Biology Chemical Centre Lund Sweden sara.linse@biochemistry.lu.se.

Chemical Science
|June 23, 2023
PubMed
Summary
This summary is machine-generated.

Many unrelated proteins can form amyloid fibrils, which are hallmarks of neurodegenerative diseases. Recent mechanistic findings are beginning to unravel the complex process of amyloid formation.

Area of Science:

  • Protein science
  • Molecular biology
  • Neurodegenerative disease research

Background:

  • A significant discovery in protein science is the propensity of diverse proteins and peptides to form amyloid fibrils in vivo and in vitro.

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  • Amyloid fibrils are recognized as pathological hallmarks of prevalent neurodegenerative diseases, such as Alzheimer's and Parkinson's.