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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Protein-Protein Interfaces

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Related Experiment Video

Updated: May 24, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Published on: March 9, 2014

Protein-protein interactions in plants.

Yoichiro Fukao¹

¹Plant Global Educational Project, Nara Institute of Science and Technology, Ikoma, Japan.

Plant & Cell Physiology

|March 3, 2012

Summary

Understanding protein-protein interactions (PPIs) is key to cellular function. Advanced mass spectrometry techniques improve PPI identification, but require validation to ensure accuracy in plant proteomics.

Area of Science:

Proteomics
Molecular Biology
Biochemistry

Background:

Protein-protein interactions (PPIs) are crucial for understanding protein functions and cellular networks.
Established methods like affinity purification and mass spectrometry (AP-MS) and yeast two-hybrid have advanced PPI analysis.
Increased protein identification via mass spectrometry (MS) has led to a higher rate of false positives.

Purpose of the Study:

To review the current status of protein-protein interaction analysis.
To discuss advanced techniques for identifying minor and transient PPIs.
To highlight future challenges in plant proteomics.

Main Methods:

Review of established PPI analysis strategies including AP-MS, yeast two-hybrid, and imaging.

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Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

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Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

Related Experiment Videos

Last Updated: May 24, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

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Published on: March 9, 2014

Identification of Post-translational Modifications of Plant Protein Complexes

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

Discussion of advanced MS-based techniques like multidimensional protein identification technology and OFFGEL electrophoresis.

Mention of filter-aided sample preparation for improved protein identification.

Main Results:

Recent advancements in MS and large-scale proteome analyses have increased protein identification.
A higher false-positive rate necessitates confirmation of PPI data using independent approaches.
New and improved methods enhance the identification of minor proteins and low-affinity PPIs.

Conclusions:

Accurate evaluation of PPI data requires validation through independent methods.
Advanced proteomic techniques are essential for identifying transient interactions and low-abundance proteins.
Future plant proteomics research faces challenges in refining PPI analysis methods.