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

No description available

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

No description available

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

You might also read

Related Articles

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

Sort by

Same author

An isotype-specific phosphorylation of Hsp90 rewires co-chaperone regulations.

The Journal of biological chemistry·2026

Same author

Optimizing LOD/LOQ and sample consumption during analytical ultracentrifugation to characterize AAV gene therapy vectors.

Journal of pharmaceutical and biomedical analysis·2026

Same author

Association-induced folding governs surrogate light chain and pre-B cell receptor core assembly.

Nature communications·2026

Same author

The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle.

Molecular cell·2025

Same author

Alternative to MSCR Test: A Novel Rheological Method for Evaluating Asphalt Mastic Performance at High Temperatures.

Materials (Basel, Switzerland)·2025

Same author

Inline optical cell alignment inspection (IOCAI) improves data quality in sedimentation-velocity analytical ultracentrifugation experiments.

Journal of pharmaceutical sciences·2025

Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026

Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026

Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026

Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026

Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026

Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 2, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

hsp90: twist and fold.

Klaus Richter¹, Johannes Buchner

¹Department of Chemistry, Technische Universität München, Germany.

|October 24, 2006

Summary

This summary is machine-generated.

Molecular chaperones like heat shock protein 90 (Hsp90) assist protein folding. New crystal structures illuminate the Hsp90 reaction cycle, revealing its mechanism for client protein maturation.

More Related Videos

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

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Related Experiment Videos

Last Updated: Apr 2, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

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

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Molecular chaperones are essential cellular machinery responsible for protein folding, preventing aggregation, and facilitating proper protein function.
Heat shock proteins, particularly Hsp90, play critical roles in cellular stress responses and the regulation of diverse signaling pathways by stabilizing client proteins.

Discussion:

The crystal structures of HtpG, an Escherichia coli Hsp90 homolog, provide atomic-level detail of its conformation.
Integration of these new structures with existing data on Hsp90-cochaperone and Hsp90-client complexes offers a comprehensive view of the Hsp90 machinery.
These structural insights are crucial for understanding the dynamic nature of the Hsp90 chaperone cycle.

Key Insights:

The reported crystal structures of HtpG offer unprecedented insights into the structural basis of Hsp90 function.
Understanding the Hsp90 reaction cycle is vital for comprehending how this chaperone facilitates the conformational maturation of its diverse client proteins.
The structural data elucidates key conformational states and transitions within the Hsp90 chaperone machine.

Outlook:

Further structural and biochemical studies will refine our understanding of Hsp90's mechanism of action.
Elucidating the Hsp90 reaction cycle may lead to the development of novel therapeutic strategies targeting Hsp90-dependent processes in diseases like cancer.
The structural information can guide the design of small molecules that modulate Hsp90 activity.