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

19.4K
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...
19.4K

You might also read

Related Articles

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

Sort by
Same author

Correction: Verde et al. Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective Responses. <i>Cells</i> 2025, <i>14</i>, 680.

Cells·2026
Same author

The E3 ligase MKRN2 prevents DRiP accumulation in stress granules and maintains granulostasis.

EMBO reports·2026
Same author

Small heat shock proteins and biomolecular condensates.

Cellular and molecular life sciences : CMLS·2026
Same author

NAC promotes co-translational protein folding at the ribosomal tunnel exit.

Molecular cell·2026
Same author

MYC-driven gliosis impairs neuron-glia communication in amyotrophic lateral sclerosis.

Brain : a journal of neurology·2025
Same author

NAC promotes co-translational protein folding at the ribosomal tunnel exit.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Dec 24, 2025

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
12:34

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments

Published on: September 16, 2016

8.0K

Studying heat shock proteins through single-molecule mechanical manipulation.

Dhawal Choudhary1,2, Laura Mediani3, Serena Carra4

  • 1Department of Physics, Informatics and Mathematics, University of Modena and Reggio Emilia, 41125, Modena, Italy.

Cell Stress & Chaperones
|April 8, 2020
PubMed
Summary

Cellular proteostasis imbalances link to aging and disease. Single-molecule force spectroscopy techniques like optical tweezers and atomic force microscopy reveal molecular chaperone mechanisms, suggesting complex roles for heat shock proteins (HSPs) and small heat shock proteins (sHSPs).

Keywords:
Heat shock proteinsMechanism of actionSingle-molecule manipulationSmall heat shock proteinsStructural dynamics

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

9.1K
Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.2K

Related Experiment Videos

Last Updated: Dec 24, 2025

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments
12:34

Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments

Published on: September 16, 2016

8.0K
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

9.1K
Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.2K

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Biophysics

Background:

  • Cellular proteostasis, crucial for preventing age-related and neurodegenerative diseases, relies on molecular chaperones like heat shock proteins (HSPs) and small heat shock proteins (sHSPs).
  • sHSPs act as a primary defense against protein misfolding, sequestering aberrant proteins for subsequent processing, refolding, or degradation, often with HSP70 system assistance.
  • Understanding chaperone molecular mechanisms is key for developing therapeutic strategies targeting aging and disease.

Purpose of the Study:

  • To elucidate the molecular mechanisms of HSPs and sHSPs in maintaining cellular proteostasis.
  • To explore the application of single-molecule force spectroscopy techniques in studying chaperone dynamics.
  • To investigate the complex physiological roles of molecular chaperones.

Main Methods:

  • Utilizing single-molecule force spectroscopy techniques, specifically optical tweezers (OT) and atomic force microscopy (AFM).
  • Describing the working principles and experimental strategies of OT and AFM for chaperone studies.
  • Analyzing single-molecule manipulation studies on HSPs and sHSPs.

Main Results:

  • Demonstrated the capability of OT and AFM to probe the structural dynamics of HSPs and sHSPs at the single-molecule level.
  • Provided insights into the key molecular mechanisms underlying chaperone activities.
  • Highlighted findings suggesting a more intricate physiological role for these chaperones than previously understood.

Conclusions:

  • Single-molecule force spectroscopy provides powerful tools for dissecting chaperone function.
  • HSPs and sHSPs exhibit complex mechanisms crucial for cellular proteostasis.
  • Further research into these chaperones may unlock novel therapeutic targets for age-related and neurodegenerative diseases.