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...

The Spindle Assembly Checkpoint

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...

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...

You might also read

Related Articles

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

Sort by

Same author

Stepwise recruitment of chaperone Hsc70 by DNAJB1 produces ordered arrays primed for bursts of amyloid fibril disassembly.

Communications biology·2025

Same author

Structural basis of substrate progression through the bacterial chaperonin cycle.

Proceedings of the National Academy of Sciences of the United States of America·2023

Same author

Sequential roles for red blood cell binding proteins enable phased commitment to invasion for malaria parasites.

Nature communications·2023

Same author

Structural journey of an insecticidal protein against western corn rootworm.

Nature communications·2023

Same author

Structural basis of ubiquitin-independent PP1 complex disassembly by p97.

The EMBO journal·2023

Same author

A structural basis for prion strain diversity.

Nature chemical biology·2023

Search research articles

Related Experiment Video

Updated: Jul 7, 2026

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

Chaperone machines in action.

Helen R Saibil¹

¹Department of Crystallography and Institute of Structural Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK. h.saibil@mail.cryst.bbk.ac.uk

Current Opinion in Structural Biology

|February 5, 2008

Summary

Molecular chaperones like Hsp60, 70, and 100 assist protein folding and prevent aggregation. Recent studies clarify their mechanisms and roles in disease and aging.

Area of Science:

Molecular biology
Cellular mechanisms
Protein homeostasis

Background:

Chaperones are essential for protein folding, unfolding, and disaggregation.
Understanding chaperone mechanisms is crucial for cellular function.
Chaperones play roles in preventing toxic protein aggregation in diseases and aging.

Purpose of the Study:

To elucidate the operational mechanisms of major chaperone families (Hsp60, 70, 100).
To explore chaperone interactions with non-native substrate proteins.
To investigate the role of chaperones in preventing toxic aggregates and their connection to aging.

Main Methods:

Structural biology insights into Hsp70 and Hsp90.
Analysis of ATP-driven mechanisms in bacterial Hsp60s.

More Related Videos

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Related Experiment Videos

Last Updated: Jul 7, 2026

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

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Review of recent advances in understanding chaperone-substrate interactions.

Main Results:

Detailed understanding of bacterial Hsp60 ATP-driven mechanisms.
Emerging structural data for Hsp70 and Hsp90 revealing allosteric mechanisms.
Improved comprehension of chaperone interactions with non-native proteins.
Advances in understanding chaperone roles in preventing aggregate formation in degenerative diseases and aging.

Conclusions:

Significant progress has been made in understanding chaperone mechanisms and functions.
Chaperones are critical for protein quality control, with implications for disease and aging.
Further research into chaperone-substrate interactions and allosteric mechanisms is ongoing.