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Amyloid Fibrils

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 Fibrils

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...

Fibrous Proteins

Fibrous Proteins

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...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Fibril-associated Collagen

Fibril-associated Collagen

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For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

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Related Experiment Video

Updated: May 31, 2026

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

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

Published on: September 17, 2017

Structural complexity of a composite amyloid fibril.

Józef R Lewandowski¹, Patrick C A van der Wel, Mike Rigney

¹Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA.

Journal of the American Chemical Society

|July 20, 2011

Summary

Amyloid fibrils are complex, with yeast prion protein Sup35p fragments forming composite protofilaments, not polymorphic ones. Crystal structures may not accurately represent fibril structures.

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Related Experiment Videos

Last Updated: May 31, 2026

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

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

Published on: September 17, 2017

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Area of Science:

Biochemistry
Structural Biology
Biophysics

Background:

Amyloid fibril structure and formation are critical for understanding diseases but remain challenging to study.
Yeast prion protein Sup35p fragment GNNQQNY forms amyloid-like crystals and fibrils, with crystals previously thought to represent fibril structure.

Purpose of the Study:

To investigate the structure and dynamics of GNNQQNY amyloid fibrils using magic-angle-spinning (MAS) NMR.
To determine if observed NMR signals indicate fibril polymorphism or a different assembly mechanism.

Main Methods:

Magic-angle-spinning (MAS) Nuclear Magnetic Resonance (NMR) spectroscopy to analyze fibril structure and dynamics.
Electron Microscopy (EM) to visualize fibril morphology.

Main Results:

GNNQQNY peptides assemble into composite protofilaments with three distinct conformations, rather than polymorphic fibrils.
Electron microscopy revealed ribbon-like fibrils formed by the combination of these protofilaments.
NMR data identified restricted side-chain conformations at interfaces, suggesting interdigitated steric zippers.

Conclusions:

Amyloid fibril structures are more complex than their corresponding crystal structures.
Extrapolation of crystal structures to amyloid fibril formation requires caution due to differing structural and dynamic properties.
Findings provide insights into the distinction between amyloid fibrils and crystals.