Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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 Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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...

Evolutionary Processes in Microbes

Evolutionary Processes in Microbes

Microbial evolution occurs rapidly due to short generation times and a variety of genetic processes, including horizontal gene transfer, mutation, recombination, and genetic drift. These mechanisms collectively enable microbes to adapt swiftly to changing environments.Horizontal gene transfer (HGT) allows genes to move between different species and occurs through three main mechanisms: conjugation, transformation, and transduction. Conjugation involves direct cell-to-cell contact for DNA...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A historical journey of metabolite-protein interaction discovery: from data harmonization to AI-driven prediction.

Briefings in bioinformatics·2026

Same author

GBP1 recruitment to actin-rich pedestals of extracellular Gram-negative bacteria promotes pyroptosis.

The EMBO journal·2026

Same author

Signed motif analysis of the Caenorhabditis elegans neuronal network reveals positive feedforward and negative feedback loops.

BMC biology·2026

Same author

Experimental assessment of AI-based interactome mapping.

Nature communications·2026

Same author

SalmonAct deciphers transcription factor regulatory activity in <i>Salmonella</i> transcriptomics.

mSystems·2026

Same author

Nematode extracellular protein interactome expands connections between signaling pathways.

Cell genomics·2026

Search research articles

Related Experiment Video

Updated: Jul 14, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Molecular chaperones: the modular evolution of cellular networks.

Tamás Korcsmáros¹, István A Kovács, Máté S Szalay

¹Department of Medical Chemistry, Semmelweis University, Budapest, Hungary.

Journal of Biosciences

|May 31, 2007

Summary

Molecular chaperones buffer genetic variation, stabilizing cellular phenotypes and regulating evolvability. They protect cells during stress by uncoupling network modules and aid in rebuilding connections afterward, informing therapeutic strategies.

More Related Videos

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

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

Related Experiment Videos

Last Updated: Jul 14, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

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

Area of Science:

Cellular Biology
Systems Biology
Evolutionary Biology

Background:

Molecular chaperones are crucial for cellular signaling and transcriptional regulation.
Recent findings highlight chaperones as genetic buffers that stabilize phenotypes.
Chaperones may act as regulators of evolvability by influencing cellular networks.

Purpose of the Study:

To elucidate the role of molecular chaperones in cellular network stability and evolution.
To understand how chaperones modulate network modularity during stress.
To explore the potential of chaperone functions in developing therapeutic and anti-aging strategies.

Main Methods:

Network analysis of chaperone interactions within cellular signaling and transcriptional regulatory networks.
Investigating chaperone behavior in modular network dynamics under stress conditions.
Computational modeling and experimental validation of chaperone-mediated network rewiring.

Main Results:

Chaperones connect network hubs and module overlaps, acting as weak links.
During stress, chaperones uncouple network modules, providing network-level protection.
Post-stress, chaperones facilitate the re-establishment of inter-modular contacts through low-affinity sampling.

Conclusions:

Chaperones are key regulators of cellular network modularity and stability.
Chaperone-mediated network dynamics offer insights into evolvability.
Understanding chaperone functions can lead to novel therapeutic and anti-aging interventions.