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...
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...
Protein Folding01:25

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 Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

Polyphosphate modulates the stress-responsive formation of functional RNA-protein condensates in bacteria and mammalian cells.

PLoS biology·2026
Same author

Microprotein Regulates G-quadruplex Driven RNA Aggregation.

bioRxiv : the preprint server for biology·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026
Same author

Biomolecular condensates sustain pH gradients at equilibrium through charge neutralization.

Nature chemistry·2026
Same author

Visualization of liquid-liquid phase transitions using a tiny G-quadruplex binding protein.

Nature communications·2025
Same author

Quantifying collective interactions in biomolecular phase separation.

Nature communications·2025

Related Experiment Video

Updated: Jun 17, 2026

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

Protein refolding by pH-triggered chaperone binding and release.

Timothy L Tapley1, Titus M Franzmann, Sumita Chakraborty

  • 1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 19, 2010
PubMed
Summary
This summary is machine-generated.

The acid stress chaperone HdeA refolds proteins in ATP-deficient bacterial compartments. It binds proteins at low pH and releases them upon neutralization, preventing aggregation without energy input.

More Related Videos

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

Related Experiment Videos

Last Updated: Jun 17, 2026

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

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Molecular chaperones typically require adenosine triphosphate (ATP) for protein folding.
  • ATP-deficient cellular compartments pose a challenge for chaperone-mediated protein folding.

Purpose of the Study:

  • To investigate the ATP-independent protein refolding mechanism of the acid stress chaperone HdeA.
  • To elucidate how HdeA functions in the ATP-deficient bacterial periplasm.

Main Methods:

  • Described a mechanism for HdeA-mediated protein refolding.
  • Investigated substrate binding and release dynamics of HdeA under varying pH conditions.

Main Results:

  • HdeA facilitates the refolding of acid-denatured proteins in an ATP-independent manner.
  • HdeA stably binds substrates at low pH, preventing aggregation.
  • pH neutralization triggers slow substrate release, maintaining low intermediate concentrations and promoting refolding.

Conclusions:

  • HdeA utilizes a unique, energy-neutral mechanism for protein refolding.
  • This mechanism involves a single substrate binding-release cycle regulated by environmental pH.
  • HdeA's function is crucial for protein homeostasis in ATP-deficient bacterial compartments.