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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Updated: Apr 22, 2026

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

Interaction analysis through proteomic phage display.

Gustav N Sundell¹, Ylva Ivarsson¹

¹Department of Chemistry-BMC, Uppsala University, P.O. Box 576, 751 23 Uppsala, Sweden.

Biomed Research International

|October 9, 2014

Summary

This summary is machine-generated.

Proteomic phage display reveals protein-protein interactions by displaying genomic DNA or cDNA on phage particles. This method aids in discovering domain-motif interactions crucial for cellular function.

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Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Phage display is a powerful technique for identifying high-affinity ligands and consensus motifs using peptide libraries.
Proteomic phage display, an underutilized approach, involves displaying expression products of genomic DNA, cDNA, or ORFs on phage particles.
Applications include antibody epitope elucidation and uncovering protein-protein interactions.

Purpose of the Study:

To review the application of proteomic phage display for uncovering protein-protein interactions.
To highlight its potential in discovering domain-motif interactions relevant to cellular function.

Main Methods:

Utilizing proteomic libraries constructed from genomic DNA, cDNA, or ORFs displayed on phage.
Focusing on the discovery of interactions between peptide binding domains and their targets.
Leveraging phage display for genome-wide scanning and ligand identification.

Main Results:

Proteomic phage display is effective for profiling specificities of peptide binding domains.
The method facilitates the identification of high-affinity ligands with inhibitor potential.
It provides consensus motifs for scanning biologically relevant ligands.

Conclusions:

Proteomic phage display offers significant potential for uncovering protein-protein interactions.
The method is particularly suited for discovering domain-motif interactions relevant to cellular function.
Further exploration of this technique is warranted for biological discovery.