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Related Concept Videos

Ligand Binding Sites02:40

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 Sites02:40

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 and Linkage00:49

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 the...
Ligand Binding and Linkage00:49

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 the...
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...
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...

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Related Experiment Video

Updated: Jul 10, 2026

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
12:23

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

Published on: August 20, 2012

Polymer-tethered ligand-receptor interactions between surfaces II.

Cheng-Zhong Zhang1, Zhen-Gang Wang

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.

Langmuir : the ACS Journal of Surfaces and Colloids
|November 16, 2007
PubMed
Summary

This study analyzes polymer-tethered ligand-receptor binding thermodynamics. It reveals how polymer conformation and binding affinity influence surface interactions, with implications for biological and bioengineering applications.

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Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
10:34

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

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Last Updated: Jul 10, 2026

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
12:23

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

Published on: August 20, 2012

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
10:34

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

Area of Science:

  • Thermodynamics
  • Polymer Physics
  • Biophysics

Background:

  • Surface interactions are crucial in biological and experimental systems.
  • Ligand-receptor binding, mediated by polymers, governs many of these interactions.
  • Understanding the thermodynamics of these complex systems is essential.

Purpose of the Study:

  • To analyze the thermodynamics of surface interactions mediated by polymer-tethered ligand-receptor binding.
  • To derive an effective binding constant considering microscopic affinity and polymer entropy.
  • To explore different scenarios of molecular mobility and their impact on interaction thermodynamics.

Main Methods:

  • Statistical thermodynamics calculations.
  • Scaling analysis for interaction features.
  • Numerical solutions for verification.
  • Density expansion for quenched cases.

Main Results:

  • An effective 2D binding constant was derived, incorporating polymer conformation entropy.
  • Interaction thermodynamics result from a balance between binding attraction and polymer confinement repulsion.
  • Three mobility scenarios (immobile, fixed density, fixed chemical potential) were analyzed.
  • Key features like adhesion range and equilibrium separation were determined.

Conclusions:

  • The study provides a thermodynamic framework for polymer-mediated surface interactions.
  • Complex interaction potentials, including double-well and tunable barriers, can arise.
  • Findings are relevant for biological processes and bioengineering design.