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Related Concept Videos

Proteomics01:33

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 proteomics...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
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Proteome-Wide Binding Affinity Profiling.

Noah Yardeny1,2, Jacob B Geri1

  • 11Department of Pharmacology, Weill Cornell Medical College, New York, NY, USA ;

Annual Review of Pharmacology and Toxicology
|July 6, 2026
PubMed
Summary

This review covers proteome-wide affinity profiling technologies. These methods measure how strongly drug compounds bind to proteins, crucial for understanding biological processes and drug development.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Proteomics

Background:

  • Ligand-protein interactions are vital for biological functions and drug efficacy.
  • Measuring the strength of these interactions (binding affinity) is key to understanding their roles in health and disease.

Purpose of the Study:

  • To review current affinity profiling technologies for measuring proteome-wide binding affinity.
  • To highlight three primary approaches used in this field.

Main Methods:

  • Protein stability-based methods: Assess ligand-induced stabilization against denaturation.
  • Proteolytic resistance-based methods: Infer binding via changes in enzymatic digestion susceptibility.
  • Derivatized probe methods: Utilize modified probes to capture and enrich ligand-protein complexes.

Main Results:

  • Affinity profiling enables the measurement of binding affinity across the entire proteome.
  • These techniques offer insights into the specificity and strength of ligand-target interactions.
  • The reviewed methods provide complementary approaches to characterizing molecular interactions.

Conclusions:

  • Affinity profiling technologies are advancing the understanding of ligand-protein interactions.
  • These methods are essential tools for drug discovery and development.
  • Further refinement of these techniques will enhance proteome-wide binding affinity measurements.