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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...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

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...

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...

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...

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Related Experiment Video

Updated: May 28, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

How fast-folding proteins fold.

Kresten Lindorff-Larsen¹, Stefano Piana, Ron O Dror

¹D. E. Shaw Research, New York, NY 10036, USA. kresten.lindorff-larsen@DEShawResearch.com

Science (New York, N.Y.)

|October 29, 2011

Summary

This summary is machine-generated.

Understanding protein folding is key in molecular biology. Simulations reveal common principles for diverse proteins spontaneously folding into native structures via predictable pathways.

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Area of Science:

Molecular Biology
Biophysics
Computational Biology

Background:

Protein folding into three-dimensional structures is a fundamental process in molecular biology.
Understanding the principles governing protein folding remains a significant scientific challenge.

Purpose of the Study:

To investigate the common principles underlying protein folding.
To simulate the spontaneous folding of diverse proteins using atomic-level detail.

Main Methods:

Atomic-level molecular dynamics simulations were performed.
Simulations ranged from 100 microseconds to 1 millisecond.
A single physics-based energy function was employed.

Main Results:

12 structurally diverse proteins spontaneously and repeatedly folded to their native structures.
The protein backbone adopted a nativelike topology early in folding.
Folding pathways were often dominated by a single route, correlated with residue propensity.

Conclusions:

Common principles govern the folding of structurally diverse proteins.
Simulations demonstrate the ability of physics-based models to recapitulate protein folding.
The order of element formation during folding is predictable and linked to the unfolded state.