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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 Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
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...

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Related Experiment Video

Updated: May 15, 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

Exploring the sequence-structure relationship for amyloid peptides.

Kyle L Morris1, Alison Rodger, Matthew R Hicks

  • 1School of Life Sciences, University of Sussex, Falmer, East Sussex BN1 9QG, UK.

The Biochemical Journal
|December 21, 2012
PubMed
Summary
This summary is machine-generated.

Amyloid fibrils, implicated in diseases and functional roles, were structurally characterized. Researchers used advanced techniques to reveal their cross-β conformation and steric-zipper features, offering insights into peptide self-assembly.

More Related Videos

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

Related Experiment Videos

Last Updated: May 15, 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
  • Biophysics

Background:

  • Amyloid fibril formation is linked to misfolding diseases and has functional roles.
  • The cross-β molecular architecture is common in amyloid-like fibrillar systems.
  • Predictive algorithms like Waltz expand the study of amyloidogenic peptides.

Purpose of the Study:

  • To characterize the structures of amyloid-like fibrils formed by three peptides identified by the Waltz algorithm.
  • To investigate the role of side chains in peptide packing and stability within fibrils.
  • To utilize these peptides as model systems for understanding sequence-structure-stability relationships in amyloid fibrils.

Main Methods:

  • Electron microscopy
  • Linear dichroism
  • Circular dichroism (CD)
  • X-ray fibre diffraction

Main Results:

  • Structural characterization of amyloid-like fibrils formed by Waltz-identified peptides.
  • Proposal of structures revealing a cross-β conformation with 'steric-zipper' features.
  • Insights into the contribution of side chains to fibril packing and stability.

Conclusions:

  • The characterized peptides serve as valuable model systems for amyloid fibril research.
  • Understanding the structural basis of amyloid formation is crucial for both disease and functional contexts.
  • The study provides a framework for relating peptide sequence to self-assembly, stability, and structure.