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

11.7K
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...
11.7K
Chromatin Packaging01:32

Chromatin Packaging

20.4K
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...
20.4K
Chromatin Packaging02:21

Chromatin Packaging

23.5K
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...
23.5K
Chromatin Packaging02:21

Chromatin Packaging

10.3K
10.3K
The Nucleosome01:19

The Nucleosome

4.9K
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...
4.9K
The Nucleosome02:33

The Nucleosome

20.0K
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...
20.0K

You might also read

Related Articles

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

Sort by
Same author

Cellular replisomes are powered by flex-fuel motors for unwinding DNA.

Nature communications·2026
Same author

Cohesin activity accelerates the homology search.

bioRxiv : the preprint server for biology·2026
Same author

A modular framework for automated segmentation and analysis of AFM imaging of chromatin organization.

Nucleic acids research·2026
Same author

Searching for sequence features that control DNA cyclizability.

PNAS nexus·2026
Same author

CSF-Seq enables transcriptome-wide profiling of cerebrospinal fluid and identifies prognostic signature of leptomeningeal disease.

bioRxiv : the preprint server for biology·2026
Same author

Intelligent fluorophores: navigating biological complexity through adaptive single-molecule imaging.

Science bulletin·2026
Same journal

Neurochondrin promotes U5 snRNP maturation by regulating AAR2 release from PRPF8.

Nucleic acids research·2026
Same journal

Elongationless start-stop elements are stress-resilient translation gates that are more repressive than uTranslons.

Nucleic acids research·2026
Same journal

Evolution of the ribosomal exit tunnel through the eyes of the nascent chain.

Nucleic acids research·2026
Same journal

Enhancing the performance and interpretability of epigenetic clocks.

Nucleic acids research·2026
Same journal

FABIAN-variant 2026: improved prediction of the effects of DNA variants on transcription factor binding.

Nucleic acids research·2026
Same journal

Structural and biochemical characterization of Grimontia hollisae thermostable direct hemolysin with DNA reveals first Vibrio hemolysin with nuclease activity.

Nucleic acids research·2026
See all related articles

Related Experiment Video

Updated: Apr 15, 2026

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

12.3K

Nucleosomes undergo slow spontaneous gaping.

Thuy T M Ngo1, Taekjip Ha2

  • 1Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801-2902, USA.

Nucleic Acids Research
|April 1, 2015
PubMed
Summary
This summary is machine-generated.

Researchers discovered a new nucleosome conformational change called "nucleosome gaping." This spontaneous DNA packaging transition occurs under physiological conditions and may impact chromatin structure and DNA transactions.

More Related Videos

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.8K
Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography
14:56

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography

Published on: May 20, 2022

4.3K

Related Experiment Videos

Last Updated: Apr 15, 2026

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

12.3K
Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.8K
Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography
14:56

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography

Published on: May 20, 2022

4.3K

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Eukaryotic DNA is packaged into nucleosomes, fundamental units of chromatin structure.
  • Nucleosomes exhibit structural diversity through variants, modifications, and conformational states like DNA breathing.
  • These structural variations are crucial for diverse cellular functions.

Purpose of the Study:

  • To identify and characterize novel conformational dynamics of nucleosomes.
  • To investigate spontaneous conformational switching under physiological conditions.

Main Methods:

  • Single-molecule Förster Resonance Energy Transfer (smFRET) was employed.
  • FRET probes were strategically placed on nucleosomal DNA.
  • Nucleosome conformation was monitored over extended periods (30-60 min) under varying ionic conditions.

Main Results:

  • A novel conformational transition, termed "nucleosome gaping," was identified.
  • Gaping involves transitions normal to the DNA plane (5-10 Å) on a minute timescale (1-10 min).
  • These gaping transitions are distinct from known nucleosome dynamics like breathing, sliding, or tightening.

Conclusions:

  • Nucleosome gaping represents a previously unobserved dynamic conformational state.
  • This transition may play a significant role in enzymatic processing of nucleosomal DNA.
  • Nucleosome gaping could influence the formation of higher-order chromatin fiber structures.