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

Recombinant DNA01:09

Recombinant DNA

92.4K
Overview
92.4K
Recombinant DNA01:09

Recombinant DNA

17.4K
17.4K
Viral Recombination00:57

Viral Recombination

22.3K
Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
22.3K

You might also read

Related Articles

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

Sort by
Same author

Uncovering Gaps in Obesity Medicine Competencies: Insights from Ten U.S. Medical Schools.

Medical science educator·2026
Same author

Spirituality as a Component of Student Resilience and Well-Being in Standards 2025.

American journal of pharmaceutical education·2026
Same author

Chemical Fingerprinting of Synthetic Polymers via Direct Insertion Probe Mass Spectrometry.

Macromolecules·2026
Same author

Metabolism matters: Interspecies variability and ecological traits of biotransformation kinetics.

Ecotoxicology and environmental safety·2026
Same author

The Role of the Omega Subzone in Determining the Membership of a Protein in One of the Two Families of the LexA/Signal Peptidase-like Superfamily.

International journal of molecular sciences·2026
Same author

Structural Basis for Trivalent Cross-Linking of a Patient-Derived IgE Antibody by the Major Peanut Allergen Ara h 2.0201.

Allergy·2026

Related Experiment Video

Updated: May 2, 2026

Engineering and Evolution of Synthetic Adeno-Associated Virus AAV Gene Therapy Vectors via DNA Family Shuffling
21:55

Engineering and Evolution of Synthetic Adeno-Associated Virus AAV Gene Therapy Vectors via DNA Family Shuffling

Published on: April 2, 2012

28.1K

A novel chimeric avidin with increased thermal stability using DNA shuffling.

Barbara Taskinen1, Tomi T Airenne2, Janne Jänis3

  • 1BioMediTech, University of Tampere, Tampere, Finland; Fimlab Laboratories, Pirkanmaa Hospital District, Tampere, Finland.

Plos One
|March 18, 2014
PubMed
Summary

Engineered avidin proteins (avidins) exhibit enhanced stability and biotin binding. Structural analysis confirmed protein fold integrity, paving the way for improved biotechnological applications.

More Related Videos

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

10.0K
Expression of Exogenous Antigens in the Mycobacterium bovis BCG Vaccine via Non-genetic Surface Decoration with the Avidin-biotin System
10:11

Expression of Exogenous Antigens in the Mycobacterium bovis BCG Vaccine via Non-genetic Surface Decoration with the Avidin-biotin System

Published on: January 31, 2018

8.7K

Related Experiment Videos

Last Updated: May 2, 2026

Engineering and Evolution of Synthetic Adeno-Associated Virus AAV Gene Therapy Vectors via DNA Family Shuffling
21:55

Engineering and Evolution of Synthetic Adeno-Associated Virus AAV Gene Therapy Vectors via DNA Family Shuffling

Published on: April 2, 2012

28.1K
Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

10.0K
Expression of Exogenous Antigens in the Mycobacterium bovis BCG Vaccine via Non-genetic Surface Decoration with the Avidin-biotin System
10:11

Expression of Exogenous Antigens in the Mycobacterium bovis BCG Vaccine via Non-genetic Surface Decoration with the Avidin-biotin System

Published on: January 31, 2018

8.7K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Avidins are versatile proteins extensively used in biotechnology.
  • Previous work demonstrated chimeric avidin creation via recombination and phage display.
  • Chimeric avidin A/A2-1 was previously selected and characterized.

Purpose of the Study:

  • To report the crystal structure of chimeric avidin A/A2-1.
  • To improve selection methods for avidins with reduced biotin dissociation rates.
  • To engineer novel chimeric avidins with enhanced thermal stability and biotin binding.

Main Methods:

  • X-ray crystallography at 1.8 Å resolution.
  • Random mutagenesis by recombination.
  • Tailored biopanning protocol (phage display).
  • Differential scanning calorimetry (DSC) for thermal stability assessment.

Main Results:

  • The crystal structure of A/A2-1 confirmed the protein fold was unaffected by sequence shuffling.
  • Improved biopanning yielded chimeric mutant A/A2-B with slower biotin dissociation.
  • A/A2-B exhibited increased thermal stability compared to parental proteins and A/A2-1, particularly at extreme pH.
  • Rational design led to A/A2-B I109K, further reducing biotin dissociation and increasing thermal stability.

Conclusions:

  • Chimeric avidin engineering can yield proteins with improved stability and binding properties.
  • Structural insights validate the functional characteristics of engineered avidins.
  • The developed methodology allows for the selection of avidins with tailored dissociation rates and enhanced stability for biotechnological applications.