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 Experiment Videos

Engineering redox functions in a nucleic acid binding protein.

Jon R Wilson1, Daren J Caruana, Gianfranco Gilardi

  • 1Department of Biological Sciences, Biochemistry Building, Imperial College, London, UK SW7 2AY.

Chemical Communications (Cambridge, England)
|March 5, 2003
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Multimodal Genotype-Phenotype Analysis in SMARCB1-Associated Developmental Disorders.

Genetics in medicine : official journal of the American College of Medical Genetics·2026
Same author

Targeting the US21 viroporin of human cytomegalovirus by calcium channel blockers as a new antiviral strategy.

Current research in microbial sciences·2026
Same author

Mimicking fenthion metabolism with human FMO3 and CYP2C19 biosensors.

Bioelectrochemistry (Amsterdam, Netherlands)·2026
Same author

Calcium as a molecular switch that regulates Annexin A11 N- and C-terminal domains interaction and its role in ALS.

International journal of biological macromolecules·2026
Same author

Binding of 14-3-3 stabilises recombinant AMPKγ2-containing complexes.

The Biochemical journal·2026
Same author

Structural Impact of 4-Hydroxynonenal Modification on Human Cytochrome CYP4F11.

ChemMedChem·2026
Same journal

An intrinsically stretchable nanowire-based sensing patch for wearable analysis of sweat chloride ion composition.

Chemical communications (Cambridge, England)·2026
Same journal

A sterically rigid-flexible balanced NHC-Pd precatalyst for room-temperature solvent-free C-N coupling of benzocyclic amines.

Chemical communications (Cambridge, England)·2026
Same journal

Portable fluorescent conjugated microporous polymer sensor coupled with a smartphone for on-site Fe<sup>3+</sup> detection in water.

Chemical communications (Cambridge, England)·2026
Same journal

Accelerated discovery of NO<sub>3</sub>RR single-atom catalysts <i>via</i> high-throughput DFT and machine learning.

Chemical communications (Cambridge, England)·2026
Same journal

Wafer-scale robust graphene electronics under industrial processing conditions.

Chemical communications (Cambridge, England)·2026
Same journal

Subnanoscale IrW oxide anodes: breaking immiscibility for high activity and durability in water electrolysis.

Chemical communications (Cambridge, England)·2026
See all related articles

Researchers engineered the nucleic acid binding protein, rop, to bind haem. This modification expands its function as a redox protein by leveraging conserved topology with existing redox proteins.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • The Rop protein is a known nucleic acid binding protein.
  • Rop exhibits conserved topology with several redox-active proteins.
  • Redox proteins are crucial for cellular electron transport and energy metabolism.

Purpose of the Study:

  • To engineer the Rop protein to acquire haem-binding capabilities.
  • To expand the functional repertoire of Rop beyond nucleic acid binding.
  • To explore the potential of Rop as a novel redox protein.

Main Methods:

  • Utilizing the conserved topological features between Rop and known redox proteins.
  • Employing protein engineering techniques to introduce haem-binding sites into the Rop structure.

Related Experiment Videos

  • Characterizing the engineered Rop protein for haem binding and redox activity.

    • Main Results:

    • Successfully engineered Rop to bind haem, demonstrating a novel function.
    • The engineered Rop protein exhibits characteristics of a redox protein.
    • The conserved topology was successfully exploited to introduce new functionality.

    Conclusions:

    • The Rop protein can be engineered to function as a haem-binding redox protein.
    • Protein topology is a valuable feature for engineering novel protein functions.
    • This study expands the utility of nucleic acid binding proteins in redox biology.