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

Immunoprecipitation01:20

Immunoprecipitation

7.9K
Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
7.9K
Affinity Chromatography01:03

Affinity Chromatography

3.5K
Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
3.5K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

8.7K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
8.7K

You might also read

Related Articles

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

Sort by
Same author

Integrative Chemical Genetics Platform Identifies Condensate Modulators Linked to Neurological Disorders.

Molecular biology of the cell·2026
Same author

A chemogenetic ligand-receptor pair for voltage-gated sodium channel subtype-selective inhibition.

bioRxiv : the preprint server for biology·2025
Same author

Engineering Protein-Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening.

Biomolecules·2025
Same author

A New Highly Specific and Soluble Protease for Precise Removal of N‑Terminal Purification Tags.

ACS omega·2025
Same author

Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.

The Journal of cell biology·2025
Same author

ADI-270: an armored allogeneic gamma delta T cell therapy designed to target CD70-expressing solid and hematologic malignancies.

Journal for immunotherapy of cancer·2025

Related Experiment Video

Updated: Mar 31, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

15.7K

A designed repeat protein as an affinity capture reagent.

Elizabeth B Speltz1, Rebecca S H Brown1, Holly S Hajare1

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.

Biochemical Society Transactions
|October 31, 2015
PubMed
Summary

Designed tetratricopeptide repeat (TPR) proteins enable efficient affinity purification. This protein engineering advance demonstrates how basic research on protein-peptide interactions can yield practical applications in reagent development.

Keywords:
affinity reagentantibodyprotein designprotein purificationprotein–protein interactionsrepeat protein

More Related Videos

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
07:53

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Published on: August 16, 2019

9.9K
Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
11:30

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells

Published on: January 26, 2017

15.7K

Related Experiment Videos

Last Updated: Mar 31, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells
10:37

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

15.7K
Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
07:53

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study

Published on: August 16, 2019

9.9K
Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
11:30

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells

Published on: January 26, 2017

15.7K

Area of Science:

  • Protein Engineering
  • Biochemistry
  • Structural Biology

Background:

  • Repeat proteins, particularly tetratricopeptide repeat (TPR) proteins, are amenable to protein engineering and design.
  • Previous studies established the ability to rationally manipulate the structure and stability of TPR proteins.
  • Research has advanced the design and characterization of peptide-binding TPR modules and their assembly into supramolecular arrays.

Purpose of the Study:

  • To develop a tetratricopeptide repeat (TPR)-peptide interaction for the practical application of affinity purification.
  • To illustrate the general utility of designed protein interactions.
  • To highlight the translation of basic research on protein-peptide interactions into novel reagents.

Main Methods:

  • Design and engineering of specific tetratricopeptide repeat (TPR) modules.
  • Characterization of designed TPR-peptide interactions.
  • Assembly of TPR modules into supramolecular arrays.
  • Application of a designed TPR-peptide interaction for affinity purification.

Main Results:

  • Successful design and characterization of peptide-binding TPR modules.
  • Demonstration of the utility of designed protein interactions for affinity purification.
  • Validation of a specific TPR-peptide interaction for a practical application.

Conclusions:

  • Designed tetratricopeptide repeat (TPR) proteins can be effectively utilized for affinity purification.
  • Basic research into protein-peptide interactions can lead to the development of novel reagents.
  • The engineered TPR-peptide interaction serves as a versatile tool with broad applicability.