Related Experiment Video
Updated: May 17, 2026
12:42
Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Similarities between protein folding and granular jamming.
Prasanth P Jose1, Ioan Andricioaei
1Department of Chemistry, University of California, Irvine, California 92697, USA.
Nature Communications
|October 25, 2012
Summary
Folded proteins share characteristics with both glassy materials and jammed systems. This study reveals universal force distributions and slowed dynamics in proteins, linking protein folding to jamming theory.
Area of Science:
- Biophysics
- Soft Matter Physics
- Computational Biology
Background:
- Granular materials and glasses exhibit jamming transitions, but unified theories are lacking due to diverse particle interactions.
- Proteins undergo folding, a complex process with implications for their function and stability.
Purpose of the Study:
- To investigate if folded proteins exhibit signatures of glassiness and jamming.
- To explore the relationship between protein folding and jamming phenomena.
- To establish a link between protein folding and jamming theory.
Main Methods:
- Utilized temperature- and force-unfolding molecular dynamics simulations.
- Analyzed interatomic force distributions during protein folding.
- Examined dynamical signatures, specifically stress relaxation dynamics.
Main Results:
- Proteins exhibit a peak in interatomic force distributions upon folding, aligning with a universal curve for jammed grains and droplets.
- Folding induces a significant slowdown in stress relaxation, a hallmark of glassy dynamics.
- Protein folding shares dynamical and force-distribution signatures with jamming transitions.
Conclusions:
- Protein folding displays characteristics common to both glassiness and jamming.
- The findings suggest a deeper connection between protein folding and jamming theory, moving beyond simple analogies.
- Results may inform the design of stable polymers and bridge protein folding research with jamming theory.
Related Concept Videos
03:03Amyloid 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:22Protein Folding
Overview
01:25Protein 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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:22Protein Folding
Overview
03:00Molecular 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...
The...
03:00Molecular 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...
The...