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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...

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Related Experiment Video

Updated: May 24, 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

The amyloid packing difference: A pairwise comparison metric for amyloid structures.

Sjors H W Scheres1

  • 1Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, UK.

Structure (London, England : 1993)
|May 22, 2026
PubMed
Summary

A new method, amyloid packing difference (APD), quantifies structural variations in amyloid proteins. This tool helps differentiate between amyloid structures linked to various neurodegenerative diseases and those specific to certain conditions.

Keywords:
amyloidscross-β packingcryo-EM structure determinationstructural comparison

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Related Experiment Videos

Last Updated: May 24, 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

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

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

Published on: March 21, 2025

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Proteins can form diverse amyloid structures, necessitating methods to compare them.
  • Understanding these structural variations is crucial for studying neurodegenerative diseases.

Purpose of the Study:

  • Introduce and validate the amyloid packing difference (APD) metric.
  • Assess APD's utility in comparing amyloid structures across different proteins and diseases.

Main Methods:

  • Developed the amyloid packing difference (APD) metric.
  • Quantified structural differences based on unique cross-β packing and side-chain orientations.
  • Applied APD to analyze structures of α-synuclein, prion protein, tau, TDP-43, TAF15, antibody light chains, and transthyretin.

Main Results:

  • APD successfully clustered α-synuclein folds, mirroring structural superposition results.
  • Amyloid structures from different neurodegenerative diseases showed APD values >20%.
  • Structures associated with the same disease had APD values <40%, while peripheral amyloidosis structures had APD >60% and transthyretin filaments had APD <25%.

Conclusions:

  • APD provides a quantitative measure for comparing amyloid structures.
  • APD values offer insights into structural similarities and differences relevant to disease classification.
  • The APD metric aids in interpreting structural comparisons for future amyloid research.