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Protein Folding

Protein Folding

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,...

Protein Organization

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 Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Related Experiment Video

Updated: Oct 11, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

A guide to studying protein aggregation.

Joëlle A J Housmans^1,2, Guiqin Wu^1,2, Joost Schymkowitz^1,2

¹Switch Laboratory, VIB Center for Brain and Disease Research, Leuven, Belgium.

The FEBS Journal

|December 4, 2021

Summary

This summary is machine-generated.

Protein aggregation, linked to diseases and biomaterials, is complex. This review guides analysis of protein aggregation and amyloid formation mechanisms for better diagnostics and applications.

Keywords:

aggregation kinetics aggregation propensity aggregation-prone region amorphous aggregates fibrils protein aggregation protein homeostasis protein stability β-sheet

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Last Updated: Oct 11, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

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Area of Science:

Biochemistry
Molecular Biology
Materials Science

Background:

Protein misfolding and instability lead to aggregate formation.
Protein aggregates are implicated in human diseases and biopharmaceutical challenges.
Functional protein aggregates have applications in biomaterials, therapeutics, and food technology.

Purpose of the Study:

To elucidate the mechanisms of protein aggregation and amyloid formation.
To provide guidance on analyzing protein aggregation processes.
To facilitate the development of diagnostic and therapeutic strategies for amyloid-associated diseases.

Main Methods:

Review of commonly investigated aspects of protein aggregation.
Summary of popular analytical methods for studying protein aggregation.
Discussion of challenges in studying the dynamic nature of protein aggregation.

Main Results:

Detailed overview of protein aggregation steps and mechanisms.
Identification of key analytical techniques for characterizing protein aggregates.
Highlighting the dual role of protein aggregates in disease and functional applications.

Conclusions:

Understanding protein aggregation is crucial for disease treatment and biomaterial development.
Knowledge of aggregation pathways aids in designing targeted diagnostics and therapeutics.
This review serves as a guide for researchers studying protein aggregation.