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

Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
The Nucleosome01:19

The Nucleosome

Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
Chromatin Packaging02:21

Chromatin Packaging

Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order structures.
Chromatin Packaging01:32

Chromatin Packaging

Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...

You might also read

Related Articles

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

Sort by
Same author

Ubiquitin ligase HcPUB30 targets HcWRKY1 to regulate monoterpenoids synthesis in Hedychium coronarium.

BMC plant biology·2026
Same author

From fragrance wheel to functional genes: a multi-omics investigation into fragrance type formation in ornamental <i>Hedychium</i> flowers.

Horticulture research·2026
Same author

Deep learning-enhanced SERS biosensing platform for the intelligent differential diagnosis of ankylosing spondylitis and osteoarthritis.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2026
Same author

Trivalent‑chromium-modified palladium catalyst supported on carbon quantum dots for rapid hydrogen production from formic acid.

Journal of colloid and interface science·2026
Same author

Systematic selection of symmetry functions for transferable neural network potentials in coarse-grained molecular modeling.

The Journal of chemical physics·2026
Same author

Seawater pearl hydrolysate alleviates perimenopausal syndrome by modulating hypothalamic and uterine ERα/MAPK/CREB signaling in ovariectomized rats.

Frontiers in pharmacology·2026
Same journal

Enhanced-Sampling Simulations Reveal Distinct Intermediates in SARS-CoV-2 FSE Pseudoknot Interconversion.

Biophysical journal·2026
Same journal

Structure-based simulations of the full Flock House virus capsid reveal pathways and energetics of an infection-critical peptide externalization event.

Biophysical journal·2026
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
Same journal

Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.

Biophysical journal·2026
Same journal

Dynamic conformations of fluorophores on self-labeling protein tags.

Biophysical journal·2026
See all related articles

Related Experiment Video

Updated: Jun 8, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Electrostatic origin of salt-induced nucleosome array compaction.

Nikolay Korolev1, Abdollah Allahverdi, Ye Yang

  • 1School of Biological Sciences, Nanyang Technological University, Singapore.

Biophysical Journal
|September 23, 2010
PubMed
Summary
This summary is machine-generated.

This study reveals how salt concentration and ion type influence chromatin folding. Understanding this is key for gene regulation and requires models that include explicit mobile ions.

More Related Videos

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
05:58

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

Published on: September 6, 2024

Related Experiment Videos

Last Updated: Jun 8, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
05:58

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

Published on: September 6, 2024

Area of Science:

  • Molecular Biology
  • Biophysics
  • Computational Biology

Background:

  • Chromatin folding and unfolding are crucial for transcription but not fully understood.
  • The salt-mediated folding of nucleosome arrays is a key aspect of chromatin compaction.

Purpose of the Study:

  • To experimentally and theoretically investigate the salt-mediated folding of chromatin.
  • To understand the role of different cations in chromatin compaction.

Main Methods:

  • Sedimentation velocity measurements were used to monitor chromatin folding.
  • Computer simulations with a coarse-grained model including explicit mobile ions were performed.

Main Results:

  • A wide range of cation concentrations (five orders of magnitude) induced maximal chromatin folding.
  • Spermine(4+) was effective at 2 μM, while Na(+) required 100 mM.
  • Simulations with explicit ions agreed with experimental data, unlike simpler models.

Conclusions:

  • Chromatin folding is dependent on cation type and concentration, exhibiting polyelectrolyte behavior.
  • Accurate theoretical models for salt-induced chromatin folding must incorporate explicit mobile ions, including ion correlation and competition effects.