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

Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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...

You might also read

Related Articles

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

Sort by
Same author

How cryoEM has advanced our understanding of bacteriophages and bacteriocins targeting Clostridioides difficile.

IUCrJ·2026
Same author

A set of genetic tools for use in <i>Clostridioides difficile</i> and related species.

Microbiology (Reading, England)·2026
Same author

<i>Escherichia coli</i> Group 2 capsules and their interplay with bacteriophages.

Frontiers in microbiology·2025
Same author

Role for RTX-family toxin HlyA of extraintestinal pathogenic <i>Escherichia coli</i> in serum resistance.

FEMS microbes·2025
Same author

Molecular mechanism of bacteriophage contraction structure of an S-layer-penetrating bacteriophage.

Life science alliance·2025
Same author

Synergy between Group 2 capsules and lipopolysaccharide underpins serum resistance in extra-intestinal pathogenic <i>Escherichia coli</i>.

Microbiology (Reading, England)·2024

Related Experiment Video

Updated: May 22, 2026

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Snap denaturation reveals dimerization by AraC-like protein Rns.

Vivienne Mahon1, Robert P Fagan, Stephen G J Smith

  • 1Department of Clinical Microbiology, School of Medicine, Trinity College Dublin, St. James's Hospital, Dublin, Ireland.

Biochimie
|May 26, 2012
PubMed
Summary

The Rns regulator in Escherichia coli dimerizes both in vivo and in vitro. A new method was developed to reduce Rns aggregation, enabling further analysis.

More Related Videos

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Related Experiment Videos

Last Updated: May 22, 2026

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
11:13

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy

Published on: August 20, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • The Rns regulator is crucial for gene expression in Escherichia coli.
  • Understanding Rns dimerization and aggregation is key to elucidating its regulatory mechanisms.
  • Previous studies have faced challenges in analyzing Rns due to its aggregation properties.

Purpose of the Study:

  • To investigate the oligomeric state of the Rns regulator in Escherichia coli.
  • To characterize the aggregation behavior of Rns in vitro.
  • To develop a method for overcoming Rns aggregation to facilitate its analysis.

Main Methods:

  • In vivo and in vitro dimerization assays were performed.
  • In vitro aggregation of Rns was observed and analyzed.
  • A novel methodology was established to ameliorate Rns aggregation.

Main Results:

  • The Rns regulator of Escherichia coli was shown to dimerize in vivo and in vitro.
  • Rns was demonstrated to form aggregates under in vitro conditions.
  • A technique was successfully developed to reduce Rns aggregation.

Conclusions:

  • Rns exists as a dimer in Escherichia coli.
  • Rns aggregation presents a challenge for biochemical analysis.
  • The developed methodology allows for improved analysis of Rns through cross-linking.