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...

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...

Bacterial Protein Maturation

Bacterial Protein Maturation

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...

Coat Assembly and GTPases

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

You might also read

Related Articles

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

Sort by

Same author

Correction: Correlation between Phase Angle and the Number of Medications in Older Inpatients: A Cross-Sectional Study.

Annals of geriatric medicine and research·2026

Same author

Scavenger receptor class B type I (SR-BI) as a potential therapeutic target in multiple myeloma.

Medical molecular morphology·2026

Same author

Identification and evaluation of citrus peel-derived polymethoxyflavonoids as natural SIRT1 activators.

Food chemistry·2026

Same author

Crystal structure of the plant GABA aminotransferase AtGABA-T from Arabidopsis thaliana.

Acta crystallographica. Section F, Structural biology communications·2026

Same author

Aggressive multiple myeloma with lymph node involvement, loss of CD138, and adipophilin-positive cytoplasmic vacuolization: a case report.

Medical molecular morphology·2026

Same author

Natural food-derived antimicrobials against beer spoilage microorganisms.

Applied microbiology and biotechnology·2026

Search research articles

Related Experiment Video

Updated: Jul 17, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

HSP90-like artificial chaperone activity based on indole beta-cyclodextrin.

Masaya Toda¹, Hideaki Itoh, Yoshihiko Kondo

¹Department of Material-Process Engineering and Applied Chemistry for Environments, Faculty of Engineering and Resource Science, Akita University, Tegata, Akita 010-8502, Japan.

Bioorganic & Medicinal Chemistry

|January 20, 2007

Summary

Indole beta-cyclodextrin (beta-1) prevents citrate synthase (CS) aggregation by forming complexes with its hydrophobic beta-sheet structures. This beta-1 acts as a beta-sheet inducer, offering superior protection compared to native beta-cyclodextrin.

More Related Videos

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Related Experiment Videos

Last Updated: Jul 17, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Area of Science:

Biochemistry
Protein Chemistry
Molecular Interactions

Background:

Protein aggregation is a significant issue in biological systems and disease.
Citrate synthase (CS) is prone to aggregation under thermal stress.
Understanding protective mechanisms against protein aggregation is crucial.

Purpose of the Study:

To investigate the anti-aggregation properties of indole beta-cyclodextrin (beta-1) on citrate synthase (CS).
To elucidate the mechanism by which beta-1 prevents CS aggregation.
To compare the efficacy of beta-1 with native beta-cyclodextrin (beta-CyD).

Main Methods:

Thermal stress assays to induce CS aggregation.
Circular Dichroism (CD) spectroscopy to analyze conformational changes.
Complex formation studies between beta-1 and CS.

Main Results:

Indole beta-cyclodextrin (beta-1) effectively prevented citrate synthase (CS) aggregation during heating.
Beta-1 formed complexes with hydrophobic regions of CS's beta-sheet structure.
CD spectra indicated that beta-1 induced conformational changes in CS.
Native beta-cyclodextrin (beta-CyD) exhibited only minor suppression of CS aggregation.

Conclusions:

Indole beta-cyclodextrin (beta-1) acts as an effective anti-aggregation agent for citrate synthase (CS) under thermal conditions.
The mechanism involves beta-1 acting as a beta-sheet inducer and forming complexes with hydrophobic segments.
Beta-1 demonstrates superior protective capabilities against CS aggregation compared to native beta-cyclodextrin.