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Related Concept Videos

The Nucleosome Core Particle02:10

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...
The Nucleosome Core Particle01:12

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...
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 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...
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...

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Related Experiment Video

Updated: May 20, 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

Structural dynamics of nucleosomes at single-molecule resolution.

John S Choy1, Tae-Hee Lee

  • 1Department of Physics, Bio-X Program, Stanford University, Stanford, CA 94305, USA. johnchoy8@gmail.com

Trends in Biochemical Sciences
|July 27, 2012
PubMed
Summary
This summary is machine-generated.

Understanding how DNA interacts with histone proteins (nucleosomes) is key for genome regulation. Single-molecule methods reveal nucleosome dynamics, advancing our knowledge of DNA accessibility for essential cellular processes.

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

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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

Related Experiment Videos

Last Updated: May 20, 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

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

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

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • The precise mechanisms by which DNA-binding proteins access DNA within nucleosomes remain largely unknown, despite decades of research following Kornberg's nucleosome model.
  • Understanding nucleosome structural dynamics is critical for deciphering genome accessibility regulation.

Purpose of the Study:

  • To review recent advances in single-molecule methods for studying nucleosome structure and dynamics.
  • To elucidate how these methods enhance our understanding of DNA transactions.

Main Methods:

  • Single-molecule biophysical techniques.
  • Analysis of ensemble data to deconvolve distinct structural states.
  • Investigating nucleosome dynamics and conformational heterogeneity.

Main Results:

  • Single-molecule approaches provide high efficiency in examining subpopulation dynamics.
  • These methods allow for the deconvolution of multiple structural states within nucleosome ensembles.
  • Advances in single-molecule techniques offer unprecedented insights into nucleosome structural heterogeneity.

Conclusions:

  • Single-molecule studies are revolutionizing the understanding of nucleosome structure and dynamics.
  • These approaches are crucial for elucidating the mechanisms governing DNA accessibility and transactions.
  • Further application of single-molecule methods will deepen our comprehension of genome regulation.