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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: Jun 16, 2026

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

Exploring the sequence determinants of amyloid structure using position-specific scoring matrices.

Sebastian Maurer-Stroh1, Maja Debulpaep, Nico Kuemmerer

  • 1VIB SWITCH Laboratory, Flanders Institute for Biotechnology and Vrije Universiteit Brussel, Brussels, Belgium.

Nature Methods
|February 16, 2010
PubMed
Summary
This summary is machine-generated.

Researchers explored protein aggregation, differentiating between amorphous and amyloid structures. They developed Waltz, a tool to identify amyloid-forming sequences, aiding in understanding protein assembly and function.

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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

Related Experiment Videos

Last Updated: Jun 16, 2026

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry
09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Protein aggregation can form amorphous or ordered amyloid structures.
  • These aggregates exhibit distinct biological properties, including chaperone interactions and degradation pathways.
  • Amyloid structure is crucial for its biological function.

Purpose of the Study:

  • To experimentally investigate the sequence space of amyloid hexapeptides.
  • To develop a computational tool for distinguishing amyloid sequences from amorphous aggregates.
  • To identify amyloid-forming regions within functional amyloids.

Main Methods:

  • Experimental exploration of hexapeptide sequence space.
  • Development of a position-specific scoring matrix (Waltz).
  • Bioinformatic analysis to identify amyloidogenic regions.

Main Results:

  • Characterization of sequence-structure relationships in protein aggregation.
  • Creation of Waltz, a web-based tool for amyloid sequence prediction.
  • Identification of novel amyloid-forming regions in functional proteins.

Conclusions:

  • Structural differences in protein aggregates dictate biological behavior.
  • Waltz effectively distinguishes amyloid from amorphous aggregates.
  • The tool aids in the study of functional amyloids and protein misfolding diseases.