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...

You might also read

Related Articles

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

Sort by

Same author

Accelerated Combinatorial Drug Design for Human Immunodeficiency Virus Resistance through Seeded Multisite λ-Dynamics.

Journal of chemical theory and computation·2026

Same author

Determinants of improved CGRP peptide binding kinetics revealed by enhanced molecular simulations.

Biophysical journal·2026

Same author

Discovery of a pyridine-piperazine-based small molecule that enhances the activity of peptidase neurolysin.

The Journal of pharmacology and experimental therapeutics·2026

Same author

Computational Drug Repurposing for Alzheimer's Disease via Sheaf Theoretic Population-Scale Analysis of snRNA-Seq Data.

Journal of medicinal chemistry·2026

Same author

Conformation Driven Enhancement of Neurolysin Activity in Presence of a Small Molecule Activator.

bioRxiv : the preprint server for biology·2026

Same author

Computational Drug Repurposing for Alzheimer's Disease via Sheaf Theoretic Population-Scale Analysis of snRNA-seq Data.

ArXiv·2025

Search research articles

Related Experiment Video

Updated: Apr 18, 2026

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

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

Published on: June 7, 2018

Multiscale modeling of a conditionally disordered pH-sensing chaperone.

Logan S Ahlstrom¹, Sean M Law¹, Alex Dickson¹

¹Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.

Journal of Molecular Biology

|January 14, 2015

Summary

The pH-sensing chaperone HdeA helps bacteria survive stomach acid by unfolding into protective monomers at low pH. This study reveals atomic-level details of HdeA's pH-triggered structural changes and stability.

Keywords:

HdeA coarse-grained modeling constant pH molecular dynamics simulation intrinsically disordered protein pH-dependent dynamics

More Related Videos

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

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

Published on: October 23, 2016

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

Related Experiment Videos

Last Updated: Apr 18, 2026

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

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

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

Published on: October 23, 2016

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

Area of Science:

Biochemistry
Structural Biology
Molecular Biophysics

Background:

Enteropathogenic bacteria face harsh stomach acid, requiring survival mechanisms.
The pH-sensing chaperone HdeA protects periplasmic proteins from acid-induced aggregation.
HdeA transitions from a dimer to disordered monomers at low pH.

Purpose of the Study:

To elucidate the pH-dependent mechanism of HdeA chaperone function.
To gain atomic-level insights into HdeA's pH-triggered structural transitions.
To understand the thermodynamics of HdeA's pH response.

Main Methods:

Multiscale modeling approach combining molecular dynamics and coarse-grained simulations.
Calculation of pK(a) values using all-atom constant pH molecular dynamics.
Analysis of pH-dependent protein stability and structural changes.

Main Results:

Identified specific "pH triggers" near helix N-termini destabilizing the HdeA dimer.
Observed anomalous high pK(a) for Glu37 at the dimer interface, influencing stability.
Characterized a partially unfolded dimeric intermediate in the pH-dependent binding pathway.

Conclusions:

The study provides atomic-level insights into HdeA's pH-sensing mechanism.
Destabilization of helix macrodipoles by protonation is a key factor in monomerization.
Findings inform experimental investigations into HdeA function and bacterial survival strategies.