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

You might also read

Related Articles

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

Sort by
Same author

Seasonal summer stress affects systemic redox homeostasis: a longitudinal marker analysis in healthy adults.

Frontiers in public health·2026
Same author

Inhaled nitric oxide in therapy of pediatric and neonatal acute respiratory distress syndrome: the good, the bad and the ugly.

Expert review of respiratory medicine·2025
Same author

hmuSTUV operon positively regulates the alginate gene cluster to mediate the pathogenicity of Pseudomonas donghuensis HYS.

International journal of biological macromolecules·2025
Same author

Research Progress on the Correlation Between Atmospheric Particulate Matter and Autism.

Journal of applied toxicology : JAT·2024
Same author

HemN2 Regulates the Virulence of <i>Pseudomonas donghuensis</i> HYS through 7-Hydroxytropolone Synthesis and Oxidative Stress.

Biology·2024
Same author

Neuropeptides affecting social behavior in mammals: Oxytocin.

Peptides·2024

Related Experiment Video

Updated: May 10, 2026

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

Measuring how much work the chaperone GroEL can do.

Nicholas C Corsepius1, George H Lorimer

  • 1Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 1, 2013
PubMed
Summary
This summary is machine-generated.

Tetramethylrhodamine (TMR) dimers report GroEL

Keywords:
allosterysubstrate protein binding problem

More Related Videos

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

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

Related Experiment Videos

Last Updated: May 10, 2026

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

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

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

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • GroEL is a molecular chaperone that facilitates protein folding.
  • GroEL undergoes allosteric transitions between T (tense) and R (relaxed) states.
  • Understanding these transitions is key to elucidating chaperonin function.

Purpose of the Study:

  • To develop a quantitative method for reporting GroEL allosteric states.
  • To use tetramethylrhodamine (TMR) dimers as reporters and surrogates for substrate protein.
  • To determine the thermodynamic parameters of GroEL allosteric transitions.

Main Methods:

  • Labeling a GroEL mutant (K242C) with TMR near the peptide-binding site.
  • Utilizing TMR dimer formation and unstacking to report T-to-R state transitions.
  • Statistical spectral analysis to quantify TMR dimers and allosteric states.
  • Applying an expanded nested cooperativity model to calculate free energies.

Main Results:

  • TMR dimers form in the T state and unstack upon ATP-induced transition to the R state.
  • TMR dimers quantitatively report the allosteric state and mimic substrate protein effects.
  • Free energies for TT to TR and TR to RR transitions were determined as 27 ± 11 and 46 ± 2 kJ/mol.
  • Free energy of TMR dimer unstacking is 2.6 ± 1.0 kJ/mol per dimer.

Conclusions:

  • TMR dimers provide a robust method for monitoring GroEL allosteric dynamics.
  • GroEL performs work during the T to R transition, consistent with the iterative annealing model.
  • This study quantifies allosteric equilibria and energy landscapes in GroEL function.