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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

9.8K
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 Organization01:13

Protein Organization

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Overview
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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 Folding01:22

Protein Folding

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Overview
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Antibody Structure01:10

Antibody Structure

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Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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Fibrous Proteins00:55

Fibrous Proteins

3.1K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Related Experiment Video

Updated: Sep 7, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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General Principles Underpinning Amyloid Structure.

Alexander I P Taylor1, Rosemary A Staniforth1

  • 1School of Biosciences, University of Sheffield, Sheffield, United Kingdom.

Frontiers in Neuroscience
|June 20, 2022
PubMed
Summary
This summary is machine-generated.

Amyloid fibrils share common structural motifs and formation principles, differing from globular proteins. These insights into amyloid structure-activity relationships offer hope for developing broad-spectrum therapeutic modifiers.

Keywords:
amide ladderamyloid structurecryo-EMneurodegenerationprotein aggregationprotein foldingssNMRsteric zipper

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Amyloid fibrils represent a distinct protein folding state with unique molecular symmetry and supramolecular organization.
  • Studying amyloid structures is challenging, but recent advances in cryo-electron microscopy (cryo-EM), solid-state nuclear magnetic resonance (ssNMR), and atomic force microscopy (AFM) provide high-resolution models.

Purpose of the Study:

  • To identify common structural motifs and underlying principles governing amyloid formation across diverse systems.
  • To develop a unified view of amyloid self-assembly, function, and pathogenesis based on shared structural features.

Main Methods:

  • Analysis of high-resolution structural models obtained from cryo-EM, ssNMR, and AFM.
  • Comparative analysis of structural features and interaction motifs in various amyloid assemblies.

Main Results:

  • Despite system-specific variations, a remarkable degree of commonality exists in amyloid structural motifs and formation principles.
  • Amyloid structures exhibit distinct molecular interaction motifs, favoring lattice-like networks (e.g., steric and polar zippers), which contribute to their long-range order.
  • Shared structural features support universal structure-activity principles governing amyloid self-assembly, function, and pathology.

Conclusions:

  • Amyloid fibrils possess fundamental, shared structural characteristics and formation principles that distinguish them from globular proteins.
  • Understanding these commonalities facilitates the development of broad-spectrum therapeutic strategies targeting amyloid function and pathology.