Related Experiment Video
Updated: Apr 1, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Peptide-Induced Amyloid-Like Conformational Transitions in Proteins
Vladimir Egorov1, Natalia Grudinina2, Andrey Vasin3
1FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17 Professor Popova Street, Saint-Petersburg 197376, Russia ; FSBI Petersburg Nuclear Physics Institute, NRC Kurchatov Institute, Orlova Roscha, Gatchina 188300, Russia.
Abstract:
Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding
Protein Organization

