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

You might also read

Related Articles

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

Sort by
Same author

Influence of dicarbonyls on kinetic characteristics of glutathione peroxidase.

Doklady. Biochemistry and biophysics·2017
Same author

Structural changes in R-phycoerythrin upon CdS quantum dot synthesis in tunnel cavities of protein molecules.

International journal of biological macromolecules·2013
Same author

Effect of cadmium sulfide quantum dots on physical properties of R-phycoerythrin as a protein matrix.

Protein and peptide letters·2012
Same author

Role of thermoinduced dissociation in interaction between alpha-crystallin as an oligomeric chaperone and glyceraldehyde-3-phosphate dehydrogenase as an oligomeric protein substrate.

Doklady. Biochemistry and biophysics·2010
Same author

Antichaperone activity of cyclodextrin derivatives.

Doklady. Biochemistry and biophysics·2009
Same author

Glycogen phosphorylase b and phosphorylase kinase binding to glycogen under molecular crowding conditions. Inhibitory effect of FAD.

Biochemistry. Biokhimiia·2009

Related Experiment Video

Updated: May 3, 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

9.7K

Antiaggregation activity of chaperones and its quantification.

B I Kurganov1

  • 1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia. kurganov@inbi.ras.ru.

Biochemistry. Biokhimiia
|February 5, 2014
PubMed
Summary

This study presents methods to quantify the anti-aggregation activity of protein and chemical chaperones. It details how to calculate aggregation rates and determine chaperone effectiveness for protein stabilization.

More Related Videos

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
In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

2.5K

Related Experiment Videos

Last Updated: May 3, 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

9.7K
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
In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

2.5K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Protein aggregation is implicated in various diseases.
  • Protein chaperones, including heat shock proteins and chemical agents, can prevent or reverse this aggregation.
  • Quantitative methods are needed to assess chaperone efficacy.

Purpose of the Study:

  • To discuss and derive methods for the quantitative estimation of anti-aggregation activity of protein and chemical chaperones.
  • To establish a framework for assessing the efficiency and stoichiometry of chaperone-protein interactions.
  • To provide a basis for comparing the protective effects of different chaperone types.

Main Methods:

  • Analysis of light scattering intensity and apparent optical absorption kinetic curves.
  • Derivation of formulas for calculating the initial rate of aggregation and lag period.
  • Determination of chaperone stoichiometry via concentration-dependent aggregation rate analysis.
  • Introduction of the [L]0.5 value to quantify chemical chaperone efficiency.

Main Results:

  • Formulas were derived to quantify protein aggregation kinetics.
  • A method was established to determine the stoichiometry of chaperone-protein complexes.
  • The [L]0.5 value was proposed as a metric for chemical chaperone efficiency.
  • Approaches for evaluating combined chaperone effects were discussed.

Conclusions:

  • Quantitative methods for assessing chaperone anti-aggregation activity are crucial.
  • The developed methods allow for detailed characterization of chaperone function and efficiency.
  • These quantitative approaches can aid in the development of novel chaperone-based therapeutics.