Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

You might also read

Related Articles

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

Sort by

Same author

Targeting granule initiation and amyloplast structure to create giant starch granules in wheat.

Science advances·2026

Same author

Understanding and modifying starch metabolism to limit yield losses in field-grown cassava.

Plant physiology·2026

Same author

Starch and tuber traits of diploid potato lines B26 and B100 and their hybrids.

BMC plant biology·2026

Same author

Maturase K forms a plastidial splicing complex with a neofunctionalized branching enzyme.

Nature communications·2026

Same author

Compound starch granule formation in grass seeds is associated with distinct temporal patterns of gene expression.

Current biology : CB·2026

Same author

Starch Synthase 3 isoforms are essential for normal starch granule initiation in wheat endosperm.

The New phytologist·2026

Search research articles

Related Experiment Video

Updated: Jun 9, 2026

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

Published on: March 19, 2010

Determining Protein-Protein Interaction with GFP-Trap Beads.

Irem Yilmazer¹, Melanie R Abt¹, Yuanyuan Liang¹

¹Institute of Molecular Plant Biology , ETH Zürich, Zürich, Switzerland.

Methods in Molecular Biology (Clifton, N.J.)

|September 15, 2022

Summary

Investigating protein-protein interactions is crucial for understanding cellular functions. This study details a method using green fluorescent protein (GFP) tagging and magnetic beads for co-immunoprecipitation in plant cells, overcoming the need for specific antibodies.

Keywords:

Co-immunoprecipitation GFP-trap Magnetic beads Protein-protein interaction

More Related Videos

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Related Experiment Videos

Last Updated: Jun 9, 2026

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces

Published on: March 19, 2010

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Identification of Protein Interaction Partners in Mammalian Cells Using SILAC-immunoprecipitation Quantitative Proteomics

Published on: July 6, 2014

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Area of Science:

Molecular Biology
Biochemistry
Plant Science

Background:

Protein-protein interactions are fundamental to cellular processes.
Co-immunoprecipitation (co-IP) is a key technique for studying these interactions.
The availability of specific antibodies for bait proteins can be a limitation in co-IP.

Purpose of the Study:

To describe a reliable method for co-immunoprecipitation of tagged proteins in plant cell extracts.
To provide an alternative to traditional co-IP when specific antibodies are unavailable.
To facilitate the study of protein interactions using fluorescent protein tags.

Main Methods:

Utilizing green fluorescent protein (GFP) as a peptide tag for a candidate protein.
Employing GFP-trap magnetic beads for the isolation of tagged proteins and their interactors.
Performing co-immunoprecipitation from crude plant cell extracts.

Main Results:

Successfully co-immunoprecipitated a fluorescently tagged candidate protein along with its interacting partners.
Demonstrated the efficacy of GFP-trap magnetic beads in capturing target proteins from plant extracts.
Provided a practical protocol for studying protein interactions in plants.

Conclusions:

Genetic fusion of peptide tags, such as GFP, offers a versatile alternative for co-IP experiments.
The described GFP-trap magnetic bead method is effective for identifying protein interactors in plant systems.
This approach enhances the study of protein-protein interactions in the absence of specific antibodies.