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

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

Protein Organization

Protein Organization

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Structure of Cadherins

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...

You might also read

Related Articles

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

Sort by

Same author

Psychosocial Burden of Multiple IgE-Mediated Food Allergies in Pediatric Patients and Caregivers in the FORWARD Study.

Nutrients·2026

Same author

Histone succinylation directly inhibits Jumonji domain demethylases and stabilizes repressive chromatin states.

bioRxiv : the preprint server for biology·2026

Same author

The GNMT N-terminus Couples Folate Feedback to Methyl-donor Homeostasis.

bioRxiv : the preprint server for biology·2026

Same author

Meeting report on FASEB protein arginine methylation: mechanism to therapeutics.

The Journal of biological chemistry·2026

Same author

Do U.S males receive contraceptive counseling during medical visits? Insights from the National Survey for Family Growth.

Contraception·2026

Same author

Food allergy severity across the world: A World Allergy Organization international survey.

The World Allergy Organization journal·2025

Search research articles

Related Experiment Video

Updated: Dec 22, 2025

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Structure of a single-chain H2A/H2B dimer.

Christopher Warren¹, Jeffrey B Bonanno¹, Steven C Almo¹

¹Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Acta Crystallographica. Section F, Structural Biology Communications

|May 2, 2020

Summary

Researchers created a novel single-chain histone dimer (scH2BH2A) to study proteins interacting with soluble histones. This tool mimics nucleosomal histone conformation, aiding structural biology of chromatin assembly and regulation.

Keywords:

H2A/H2B dimer Xenopus laevis chromatin crystallography histones

More Related Videos

Analyzing and Building Nucleic Acid Structures with 3DNA

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Related Experiment Videos

Last Updated: Dec 22, 2025

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Analyzing and Building Nucleic Acid Structures with 3DNA

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Area of Science:

Molecular Biology
Structural Biology
Genomics

Background:

Chromatin, the eukaryotic genome's form, comprises DNA and proteins, with nucleosomes as fundamental units.
Histones (H2A, H2B, H3, H4) form nucleosomes, but soluble histone dimers and tetramers exist before assembly.
Understanding interactions with soluble histones is crucial but limited by a lack of structural tools.

Purpose of the Study:

To develop a novel structural tool for studying non-nucleosomal histones.
To investigate the structure of soluble histone dimers.

Main Methods:

Engineered a single-chain, tailless Xenopus H2A/H2B dimer (scH2BH2A) by fusing H2B to H2A.
Expressed and purified the scH2BH2A construct under non-denaturing conditions in bacteria.
Determined the crystal structure of scH2BH2A at 1.31 Å resolution.

Main Results:

The scH2BH2A construct was successfully expressed and purified.
The crystal structure revealed that scH2BH2A adopts a conformation highly similar to nucleosomal H2A/H2B dimers.
This indicates the engineered dimer is structurally stable and relevant.

Conclusions:

The scH2BH2A construct serves as a valuable tool for structural studies.
Facilitates research on proteins interacting with soluble H2A/H2B dimers.
Advances understanding of chromatin assembly and regulation dynamics.