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

21.1K
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...
21.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.8K
15.8K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

737
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...
737
Protein Folding01:25

Protein Folding

12.8K
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...
12.8K
Protein Folding01:22

Protein Folding

131.5K
Overview
131.5K
Protein Folding01:22

Protein Folding

36.8K
36.8K

You might also read

Related Articles

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

Sort by
Same author

BAM-BepA complexes in outer membrane protein quality control.

Nature communications·2026
Same author

Author Correction: High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs.

Nature chemistry·2026
Same author

Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers.

Analytical chemistry·2026
Same author

Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.

Chemical reviews·2026
Same author

Checking in on proteostasis.

Nature structural & molecular biology·2026
Same author

Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.

Current opinion in structural biology·2026

Related Experiment Video

Updated: Apr 19, 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

9.4K

How TriC folds tricky proteins.

Anastasia Zhuravleva1, Sheena E Radford1

  • 1Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK.

Cell
|December 7, 2014
PubMed
Summary

Chaperonins, like TRiC, help complex proteins fold correctly. New research identifies novel TRiC substrates and reveals how its subunits enable broader substrate recognition and guided protein folding.

Area of Science:

  • Molecular Biology
  • Protein Folding Mechanisms
  • Cellular Chaperone Systems

Background:

  • Chaperonins are essential molecular machines that assist protein folding within cells.
  • Understanding the substrate specificity and folding mechanisms of chaperonins is crucial for cell biology.
  • The Tri-CCT chaperonin (TRiC) is a key player in folding non-native proteins.

Purpose of the Study:

  • To identify novel substrates of the TRiC chaperonin.
  • To elucidate how TRiC utilizes its distinct subunits to expand its substrate repertoire.
  • To reveal the mechanisms by which TRiC directs productive protein folding.

Main Methods:

  • Identification and characterization of new TRiC-binding proteins.
  • Biochemical and biophysical analyses of TRiC-substrate interactions.

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

11.2K
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

3.4K

Related Experiment Videos

Last Updated: Apr 19, 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

9.4K
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

11.2K
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

3.4K
  • Structural studies to understand subunit involvement in substrate recognition.

    • Main Results:

    • A new class of TRiC substrates has been identified.
    • Evidence shows TRiC's subunits contribute to recognizing a wider range of substrates.
    • Mechanisms for TRiC's directed and productive folding of these substrates are elucidated.

    Conclusions:

    • TRiC possesses a broader substrate specificity than previously known.
    • The specific subunits of TRiC play critical roles in substrate recognition and folding.
    • This work deepens our understanding of chaperonin-mediated protein folding in vivo.