Related Experiment Video

Updated: Jun 16, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Patterns of protein unfolding and protein aggregation in ionic liquids

Diana Constatinescu1, Christian Herrmann, Hermann Weingärtner

  • 1Department of Physical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr-University, D-44780 Bochum, Germany.

Physical Chemistry Chemical Physics : PCCP
|February 11, 2010
PubMed

More Related Videos

4D Imaging of Protein Aggregation in Live Cells08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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...
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

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...
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...
The Colloidal State01:29

The Colloidal State

The formation of a colloidal system is exemplified by an aqueous solution containing Cl− ions is introduced to another containing Ag+ ions, resulting in the precipitation of solid AgCl as extremely tiny crystals. Instead of settling out as a filterable precipitate, these crystals remain suspended in the liquid, showcasing a colloidal system.A colloidal system involves colloidal particles within the approximate range of 1 to 1000 nm in at least one dimension, dispersed in a medium called the...