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

14.7K
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...
14.7K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.2K
14.2K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

744
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...
744
Amyloid Fibrils03:03

Amyloid Fibrils

10.2K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
10.2K
Protein Folding01:25

Protein Folding

8.8K
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...
8.8K
Protein Folding01:22

Protein Folding

112.3K
Overview
112.3K

You might also read

Related Articles

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

Sort by
Same author

Integrated omics reveal a unique antibacterial mechanism of action for the small molecule HSI#6.

Current research in microbial sciences·2026
Same author

Calcium controls type III secretion switch through an SctV-SctW interplay.

Frontiers in microbiology·2026
Same author

AI-Enhanced Adaptive Virtual Screening Platform Enabling Exploration of 69 Billion Molecules Discovers Structurally Validated FSP1 Inhibitors.

bioRxiv : the preprint server for biology·2026
Same author

A small molecule allosterically activates SecA dependent secretion.

Communications biology·2026
Same author

Probing Submillisecond-to-Millisecond Time Scale Conformational Dynamics in High-Molecular-Weight Biomolecules via <sup>15</sup>N Clean Transverse-Relaxation-Optimized Chemical Exchange Saturation Transfer (TROSY-CEST).

The journal of physical chemistry letters·2025
Same author

Conformational landscape adaptations enable processive phosphorylation by Src family kinases.

Science (New York, N.Y.)·2025

Related Experiment Video

Updated: Apr 30, 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

8.1K

Structural basis for protein antiaggregation activity of the trigger factor chaperone.

Tomohide Saio1, Xiao Guan, Paolo Rossi

  • 1Center for Integrative Proteomics Research and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.

Science (New York, N.Y.)
|May 10, 2014
PubMed
Summary

Molecular chaperones like trigger factor (TF) bind unfolded proteins using multiple sites and dynamic interactions. This multivalent binding prevents protein aggregation and misfolding.

More Related Videos

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

3.7K
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

2.1K

Related Experiment Videos

Last Updated: Apr 30, 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

8.1K
Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

3.7K
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

2.1K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Molecular chaperones are crucial for preventing protein aggregation and misfolding.
  • Limited structural data hinders understanding of chaperone-substrate interactions and anti-aggregation mechanisms.

Purpose of the Study:

  • To elucidate the structural, dynamic, and energetic mechanisms of trigger factor (TF) chaperone binding to unfolded alkaline phosphatase (PhoA).

Main Methods:

  • Solution structure determination using Nuclear Magnetic Resonance (NMR) spectroscopy.
  • NMR relaxation experiments to analyze protein dynamics and interactions.
  • Energetic analysis of chaperone-substrate complex formation.

Main Results:

  • TF binds to multiple regions of unfolded PhoA via predominantly hydrophobic contacts.
  • TF-PhoA interaction is highly dynamic, becoming more stable with increased binding sites and length.
  • Multivalent binding maintains the substrate protein in an extended, unfolded conformation.

Conclusions:

  • Molecular chaperones recognize unfolded polypeptides through multivalent, dynamic interactions.
  • TF acts as an unfoldase and holdase, preventing protein aggregation and premature misfolding.