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Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Ligand Binding Sites

Ligand Binding Sites

No description available

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...

Ligand Binding and Linkage

Ligand Binding and Linkage

No description available

The Equilibrium Binding Constant and Binding Strength

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:

Electron Affinity

Electron Affinity

The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).

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Updated: Jan 29, 2026

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

Affinity screening using competitive binding with fluorine-19 hyperpolarized ligands.

Yaewon Kim¹, Christian Hilty

¹Department of Chemistry, Texas A & M University, College Station, TX 77843 (USA).

Angewandte Chemie (International Ed. in English)

|February 24, 2015

Summary

This summary is machine-generated.

Fluorine-19 NMR with hyperpolarization enables rapid drug screening by measuring ligand binding affinity without titration. This method efficiently quantifies dissociation constants (K(D)) for non-fluorinated compounds using a competitive binding assay.

Keywords:

NMR spectroscopy drug discovery hyperpolarization protein-ligand interaction

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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Area of Science:

Biochemistry
Chemical Biology
Nuclear Magnetic Resonance Spectroscopy

Background:

Nuclear Magnetic Resonance (NMR) is a vital tool in drug discovery.
Hyperpolarization significantly enhances NMR signal sensitivity.
Efficient drug screening requires accurate measurement of ligand binding affinities.

Purpose of the Study:

To develop a rapid drug screening method using Fluorine-19 NMR and hyperpolarization.
To measure ligand dissociation constants (K(D)) without performing ligand titrations.
To demonstrate the utility of the method for characterizing ligand binding to trypsin.

Main Methods:

Utilized hyperpolarized Fluorine-19 NMR spectroscopy.
Employed a competitive equilibrium assay with a fluorinated reporter ligand.
Applied a single-scan Carr-Purcell-Meiboom-Gill (CPMG) experiment.
Validated the method by characterizing ligand binding to the serine protease trypsin.

Main Results:

Successfully measured dissociation constants (K(D)) for three ligands with varying affinities for trypsin.
Demonstrated that optimal accuracy is achieved when approximately 50% of the reporter ligand is displaced.
Showed that the method is applicable across a wide range of ligand affinities.

Conclusions:

Hyperpolarized Fluorine-19 NMR provides a sensitive and efficient platform for drug screening.
The competitive binding assay allows for rapid K(D) determination without titration.
This technique facilitates the screening of non-fluorinated compounds when a suitable fluorinated ligand is available.