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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.6K
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...
19.6K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
From DNA to Protein03:06

From DNA to Protein

22.4K
The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
22.4K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.7K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.7K
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

11.2K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
11.2K
DNA Helicases00:55

DNA Helicases

24.2K
DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
24.2K

You might also read

Related Articles

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

Sort by
Same author

American science at 250.

Science (New York, N.Y.)·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

Selective control of ligand binding through a distal mutation that alters the protein native ensemble.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Local and Global Breathing Motions Prime the Access to Buried Binding Site in an Antibiotic-Sequestering Protein.

ACS bio & med chem Au·2025
Same author

Virus Propagation Linked to Exceedingly Rare Gene-Expression Errors: A Single-Molecule Microscopy Demonstration.

ACS chemical biology·2025

Related Experiment Video

Updated: Feb 6, 2026

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

11.2K

Tunable order-disorder continuum in protein-DNA interactions.

Sneha Munshi1, Soundhararajan Gopi1, Gitanjali Asampille2

  • 1Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India.

Nucleic Acids Research
|August 15, 2018
PubMed
Summary

DNA-binding protein domains (DBDs) sense DNA's electric potential. The cytidine repressor (CytR) acts as an electrostatic sensor, utilizing DNA's charge for rapid, specific binding via a novel mechanism.

More Related Videos

CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

7.7K
Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
08:42

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example

Published on: October 26, 2016

12.8K

Related Experiment Videos

Last Updated: Feb 6, 2026

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

11.2K
CD Spectroscopy to Study DNA-Protein Interactions
06:48

CD Spectroscopy to Study DNA-Protein Interactions

Published on: February 10, 2022

7.7K
Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
08:42

Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example

Published on: October 26, 2016

12.8K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • DNA-binding protein domains (DBDs) explore various conformations to find specific DNA sites.
  • The strong electric potential from DNA's phosphate groups is hypothesized to be crucial for DBD function.

Purpose of the Study:

  • To investigate if DBDs have co-evolved to sense and utilize DNA's electric potential.
  • To model the intrinsically disordered DBD of cytidine repressor (CytR) as a sensor system.

Main Methods:

  • Utilized CytR as a model system, increasing solution osmolarity to mimic DNA phosphate screening.
  • Employed electrostatic calculations and an Ising-like statistical mechanical model.
  • Analyzed CytR's structural, stability, and folding rate changes.

Main Results:

  • CytR demonstrated features of an electric potential sensor, modulating its structure and landscape in a distance-dependent manner.
  • DNA acted as a non-specific macromolecular chaperone.
  • CytR exhibited an electrostatic-steering binding mechanism, binding its natural site and random DNA rapidly.

Conclusions:

  • DBDs can act as natural electrostatic potential sensors.
  • A novel binding mechanism driven by electrostatic frustration and disorder was identified.
  • DNA promotes distance-dependent protein structural transitions essential for specific and non-specific DNA binding.