Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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 Folding03:00

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...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Bacterial Protein Maturation01:26

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

Characterization Standard for <i>In-situ</i> Cryo-electron Tomography.

bioRxiv : the preprint server for biology·2026
Same author

AreTomoLive: automated reconstruction of comprehensively corrected and denoised cryo-electron tomograms in real time and at high throughput.

Nature methods·2026
Same author

Evaluating the Volta phase plate for improved tomogram alignment in cryo-electron tomography.

IUCrJ·2026
Same author

Cathepsin C-Catalyzed Ligation Generates Intralysosomal Amyloid Fibrils from Dipeptide Esters.

bioRxiv : the preprint server for biology·2026
Same author

A novel lncRNA FAM151B-DT regulates degradation of aggregation prone proteins.

Molecular psychiatry·2025
Same author

The complex developmental mechanisms of nucleus-forming jumbo phages.

Current opinion in microbiology·2025

Related Experiment Video

Updated: Jun 3, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.

Timothy O Street1, Laura A Lavery, David A Agard

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158-2517, USA.

Molecular Cell
|April 9, 2011
PubMed
Summary

Heat shock protein 90 (Hsp90) binds structured regions of unfolded proteins, altering its conformation. This interaction accelerates nucleotide-driven transitions and stimulates ATP hydrolysis, revealing Hsp90

More Related Videos

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

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

Published on: June 7, 2018

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Related Experiment Videos

Last Updated: Jun 3, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

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

Published on: June 7, 2018

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone with significant conformational flexibility.
  • The functional implications of Hsp90's conformational plasticity remain largely unexplored.
  • Understanding Hsp90's interaction with substrates is key to elucidating its chaperone mechanism.

Purpose of the Study:

  • To investigate the structural consequences of substrate binding on Hsp90 conformation.
  • To explore how substrate interaction influences Hsp90's functional dynamics.
  • To determine the binding site and affinity of Hsp90 for a model substrate.

Main Methods:

  • Small-angle X-ray scattering (SAXS) to monitor Hsp90 conformational changes.
  • Förster resonance energy transfer (FRET) to track nucleotide-driven transitions.
  • Nuclear magnetic resonance (NMR) spectroscopy to identify binding interfaces.

Main Results:

  • Hsp90 adopts a partially closed conformation around the substrate (Δ131Δ) in its apo state.
  • AMPPNP binding enhances Δ131Δ affinity and promotes a fully closed Hsp90 state.
  • Substrate binding accelerates Hsp90's open/closed transitions and stimulates ATP hydrolysis.
  • Hsp90 specifically binds to a structured region within the globally unfolded substrate.

Conclusions:

  • Hsp90 preferentially binds to locally structured regions of unfolded proteins.
  • Substrate binding acts as a key allosteric effector, modulating Hsp90's conformational cycle.
  • This interaction lowers a rate-limiting barrier, facilitating Hsp90's chaperone function.