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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...

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Updated: Jun 3, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Amyloid structure: conformational diversity and consequences.

Brandon H Toyama1, Jonathan S Weissman

  • 1Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California, San Francisco and California Institute for Quantitative Biomedical Research, San Francisco, California 94158-2542, USA. btoyama@salk.edu

Annual Review of Biochemistry
|April 5, 2011
PubMed
Summary
This summary is machine-generated.

Most proteins can form self-propagating amyloid aggregates, implicated in diseases and prion inheritance. Recent high-resolution techniques reveal diverse amyloid structures, even from identical proteins, leading to distinct heritable prion strains.

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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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Last Updated: Jun 3, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Proteins can form self-propagating, beta-sheet (amyloid) aggregates.
  • Amyloid aggregates are associated with various diseases and prion-based inheritance.
  • Understanding amyloid structure is crucial due to their disease relevance.

Purpose of the Study:

  • To explore the structural diversity of amyloid aggregates.
  • To investigate how different primary structures lead to similar amyloid architectures.
  • To understand the molecular basis of prion strains.

Main Methods:

  • Hydrogen-deuterium exchange
  • X-ray crystallography
  • Solid-state nuclear magnetic resonance (SSNMR)
  • Cryoelectron microscopy (cryoEM)

Main Results:

  • Despite divergent primary structures, amyloids share common structural features.
  • High-resolution studies reveal significant molecular-level structural diversity in amyloids.
  • Identical polypeptides can adopt multiple distinct amyloid conformations.
  • This structural polymorphism underlies distinct heritable prion states (strains).

Conclusions:

  • Amyloid structures are more diverse than previously thought.
  • Polymorphism in amyloid conformation is a key determinant of prion strain diversity.
  • Advanced biophysical methods are essential for elucidating complex amyloid structures.