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

Protein Folding

Protein Folding

Protein Folding

Protein Folding

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...

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...

Hydrolysis

Hydrolysis

Overview
Hydrolysis is a chemical reaction in which the addition of water breaks down a polymer into its simpler monomer units. For example, peptides break into amino acids, carbohydrates into simple sugars, and DNA into nucleotides. Enzymes often facilitate these processes.
Hydrolysis Reverses Dehydration Synthesis
Complex carbohydrates can be broken down by breaking the bonds between individual sugar units. The reaction breaks a glycosidic bond as water is added to the compound. The...

Step-Growth Polymerization: Overview

Step-Growth Polymerization: Overview

Step-growth or condensation polymerization is a stepwise reaction of bi or multifunctional monomers to form long-chain polymers. As all the monomers are reactive, most of the monomers are consumed at the early stages of the reaction to form small chains of reactive oligomers, which then combine to form long polymer chains in the late stages. Hence, the reaction has to proceed for a long time to achieve high molecular weight polymers.
Many natural and synthetic polymers are produced by...

Cationic Chain-Growth Polymerization: Mechanism

Cationic Chain-Growth Polymerization: Mechanism

The cationic polymerization mechanism consists of three steps: initiation, propagation, and termination. In the initiation step of the polymerization process, the π bond of a monomer gets protonated by the Lewis acid catalyst, which is formed from boron trifluoride and water. The protonation of the π bond generates a carbocation stabilized by the electron‐donating group. In the propagation step, the π bond of the second monomer acts as a nucleophile and attacks the generated carbocation,...

You might also read

Related Articles

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

Sort by

Same author

MDNA : a software module for DNA structure generation and analysis.

Nucleic acids research·2026

Same author

Small Molecule Activators of Protein Phosphatase 2A Exert Global Stabilizing Effects on the Scaffold PR65.

JACS Au·2026

Same author

Nucleation of NaCl crystals from solution: Rate prediction and influence of noisy order parameters on the committor.

The Journal of chemical physics·2026

Same author

GerAB residues predicted to interact with water based on MD simulations mediate germinosome stability in <i>Bacillus subtilis</i> spores.

Frontiers in microbiology·2026

Same author

Understanding Mechanisms of Molecular Rare Events from Start to Finish.

Physical review letters·2026

Same author

Calmodulin assists during co-translational folding of the K<sub>V</sub>7.2 channel calcium responsive domain.

Protein science : a publication of the Protein Society·2026

Search research articles

Related Experiment Video

Updated: May 12, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

Hydrophobic collapse of trigger factor monomer in solution.

Kushagra Singhal¹, Jocelyne Vreede, Alireza Mashaghi

¹van 't Hoff Institute of Molecular Sciences, University of Amsterdam, Amsterdam, The Netherlands.

|April 9, 2013

Summary

Trigger factor (TF) chaperone dynamics in solution reveal domain collapse via hydrophobic and hydrophilic interactions. This structural insight is key to understanding TF

More Related Videos

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Related Experiment Videos

Last Updated: May 12, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Trigger factor (TF) is a bacterial and chloroplast chaperone.
TF interacts with nascent polypeptide chains to prevent aggregation.
The crystal structure of TF is known, but its solution structure and dynamics remain unclear.

Purpose of the Study:

To investigate the solution structure and dynamics of Trigger factor.
To understand the interactions and conformational changes of TF domains in solution.

Main Methods:

Multiple molecular dynamics simulations were performed on Trigger factor in solution.
Hydrophobicity analysis of domain surfaces using the hydrophobic probe method.

Main Results:

TF domains exhibit collective motions hinged at inter-domain linkers with preserved secondary structure.
Isolated TF adopts a collapsed state through domain pairing, driven by hydrophobic and stabilized by hydrophilic contacts.
Domain pairing alters TF's hydrophobic map, making specific domain pairs more hydrophilic or hydrophobic.

Conclusions:

The study provides insights into the dynamic behavior and domain interactions of Trigger factor in solution.
Understanding TF's solution structure and dynamics is crucial for elucidating its chaperone function and substrate interactions.