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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 the...

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 the...

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:

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:

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Related Experiment Video

Updated: May 30, 2026

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

Published on: November 2, 2011

Influence of binding groups on molecular junction formation.

Carlos R Arroyo¹, Edmund Leary, Andrés Castellanos-Gómez

¹Departamento de Física de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain.

Journal of the American Chemical Society

|August 3, 2011

Summary

This study reveals how gold atom rearrangements in molecular junctions influence their formation. Thiols significantly alter gold electrode dynamics more than amines, a key factor for binding group selection.

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Area of Science:

Materials Science
Surface Chemistry
Nanotechnology

Background:

Understanding molecular junction formation is crucial for molecular electronics.
Gold-atom rearrangements in electrodes can significantly impact junction properties.

Purpose of the Study:

To investigate the role of gold-atom rearrangements in the formation mechanism of molecular junctions.
To compare the influence of different binding groups (thiols vs. amines) on electrode dynamics.

Main Methods:

Utilizing break-junction experiments to form and analyze molecular junctions.
Analyzing junction stretching length, plateau lengths, and gold one-atom contact lengths.

Main Results:

Gold-atom rearrangements were found to be a significant factor in molecular junction formation.
Alkane dithiols induced more substantial changes in gold electrode dynamics compared to diamines.

Conclusions:

The binding group significantly influences electrode dynamics during molecular junction formation.
Thiols have a greater impact on gold electrode dynamics than amines, which must be considered when selecting binding groups for molecular devices.