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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...

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

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Related Experiment Video

Updated: May 10, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Chaperonin-mediated protein folding.

Arthur L Horwich¹

¹Howard Hughes Medical Institute, Yale School of Medicine, New Haven, Connecticut 06510, USA. arthur.horwich@yale.edu

The Journal of Biological Chemistry

|June 28, 2013

Summary

Chaperonins are crucial for protein folding. Decades of research have elucidated their structure and mechanism, leading to significant discoveries in molecular biology.

Area of Science:

Biochemistry and Molecular Biology
Structural Biology
Protein Dynamics

Background:

Chaperonins are essential molecular machines involved in protein folding.
Research over twenty years has focused on their function, structure, and mechanism.
This work was recently recognized with the 2013 Herbert Tabor Award.

Discussion:

The abstract highlights key findings from two decades of chaperonin research.
It emphasizes the collaborative nature of scientific discovery.
The narrative connects personal collaborations with scientific advancements.

Key Insights:

Elucidation of chaperonin action in protein folding.
Detailed analysis of chaperonin structure.
Understanding the mechanism of chaperonin-assisted protein folding.

Keywords:

Chaperone Chaperonin Molecular Chaperone Polypeptide Protein Folding Protein Misfolding Yeast

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Last Updated: May 10, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Outlook:

Continued exploration of chaperonin roles in cellular processes.
Investigating chaperonin interactions with other cellular components.
Applying chaperonin knowledge to protein misfolding diseases.