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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: Jul 4, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

The protein folding problem.

Ken A Dill¹, S Banu Ozkan, M Scott Shell

¹Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143, USA. dill@maxwell.ucsf.edu

Annual Review of Biophysics

|June 25, 2008

Summary

This summary is machine-generated.

The protein folding problem is being solved through computational prediction and a new understanding of folding mechanisms. Proteins are now designed routinely, with structures accurately predicted for small proteins using computer methods.

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Last Updated: Jul 4, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

4D Imaging of Protein Aggregation in Live Cells

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Area of Science:

Biochemistry
Computational Biology
Structural Biology

Background:

The protein folding problem encompasses understanding the folding code, mechanism, and structure prediction from amino acid sequences.
Historically a grand challenge, significant advancements have been made in recent years.

Purpose of the Study:

To summarize recent progress in protein folding research.
To present a testable explanation for rapid protein folding.
To highlight the design and application of novel proteins and polymers.

Main Methods:

Computational methods for structure prediction.
Design of foldable proteins and nonbiological polymers.
Analysis of protein folding as a series of local optimization problems.

Main Results:

Small protein structures are now frequently well-predicted by computational approaches.
Foldable proteins and nonbiological polymers are being routinely designed.
A testable hypothesis for rapid protein folding has been proposed.

Conclusions:

Protein folding is increasingly understood, with computational tools aiding structure prediction.
The proposed mechanism suggests proteins fold by solving smaller, sequential optimization problems.
Advances facilitate the routine design and application of novel protein structures.