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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...

Protein Folding

Protein Folding

Protein Folding

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...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...

Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

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Related Experiment Video

Updated: Jul 19, 2026

Amyloid and the Cross-Beta Architecture

Amyloid and the Cross-Beta Architecture

Published on: February 13, 2026

Computational approaches to fibril structure and formation.

Carol K Hall¹, Victoria A Wagoner

¹Chemical Engineering Department, North Carolina State University, Raleigh, 27695, USA.

Methods in Enzymology

|October 19, 2006

Summary

Protein misfolding into amyloid fibrils contributes to human diseases. Computational simulations, including molecular dynamics, offer insights into fibril structure and formation, aiding disease research.

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Area of Science:

Biochemistry and Molecular Biology
Computational Biology
Neuroscience

Background:

Amyloid fibril formation from soluble proteins is implicated in various human diseases.
The insoluble nature of amyloid fibrils presents experimental challenges for structural studies.

Purpose of the Study:

To investigate the molecular mechanisms of amyloid fibril formation and structure.
To utilize computational approaches for studying insoluble protein aggregates.

Main Methods:

Employed intermediate-resolution discontinuous molecular dynamics (MD) simulations.
Utilized atomistic molecular dynamics (MD) simulations.
Combined strengths of different simulation resolutions for comprehensive analysis.

Main Results:

Provided a detailed molecular-level understanding of amyloid fibril structure.
Elucidated key aspects of the fibril formation process.
Demonstrated the utility of integrated computational methods.

Conclusions:

Computational simulations are valuable tools for studying amyloid fibril formation and structure.
A combined approach using different MD resolutions yields a robust molecular picture.
Findings contribute to understanding disease mechanisms linked to protein aggregation.