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-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Aqueous Solutions and Heats of Hydration

Aqueous Solutions and Heats of Hydration

Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

You might also read

Related Articles

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

Sort by

Same author

The RecBCD complex interacts directly with the DNA sliding clamp in Escherichia coli.

Nucleic acids research·2026

Same author

Cooperativity, dynamics, and the free-energy surfaces of charge-patterned IDPs.

bioRxiv : the preprint server for biology·2026

Same author

Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).

bioRxiv : the preprint server for biology·2026

Same author

Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins.

JACS Au·2026

Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026

Same author

Does body weight affect body self-image perception among tribal adolescent girls and boys?

Anthropologischer Anzeiger; Bericht uber die biologisch-anthropologische Literatur·2026

Search research articles

Related Experiment Video

Updated: Nov 30, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes.

Andrea Sottini¹, Alessandro Borgia^1,2, Madeleine B Borgia^1,2

¹Department of Biochemistry, University of Zurich, Zurich, Switzerland.

Nature Communications

|November 13, 2020

Summary

Highly charged disordered proteins form stable complexes. At high concentrations, transient complexes enable rapid association/dissociation, maintaining biological network responsiveness.

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Related Experiment Videos

Last Updated: Nov 30, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

Area of Science:

Biochemistry
Biophysics
Molecular Biology

Background:

Intrinsically disordered proteins (IDPs) can form high-affinity complexes while retaining disorder.
The interaction between linker histone H1.0 and prothymosin α demonstrates unusual concentration-dependent kinetics.

Purpose of the Study:

To elucidate the mechanism behind the concentration-dependent switch in association/dissociation kinetics of highly charged IDPs.
To explain how transient ternary complex formation influences binding kinetics.

Main Methods:

Utilized molecular simulations to investigate the dynamics of protein complexes.
Analyzed the formation and role of transient ternary complexes.

Main Results:

Identified transient ternary complex formation as the driver for accelerated exchange kinetics at high protein concentrations.
Demonstrated that protein disorder facilitates diffusion-limited binding and rapid monomer exchange via competitive substitution.
Observed a switch from slow to fast exchange kinetics with increasing protein concentration.

Conclusions:

Transient ternary complexes in disordered polyelectrolyte complexes enable rapid kinetics despite high binding affinities.
Biological polyelectrolytes can maintain responsive regulatory networks through these dynamic interactions.