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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 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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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:
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:
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...

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A Method for Selecting Structure-switching Aptamers Applied to a Colorimetric Gold Nanoparticle Assay
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Published on: February 28, 2015

Kinetic Superselectivity in Multivalent Binding.

Vid Ravnik1, Baptiste Chabaud2, Urban Bren1,3,4

  • 1Faculty of Chemistry and Chemical Engineering, University of Maribor, Smetanova ulica 17, 2000 Maribor, Slovenia.

The Journal of Physical Chemistry Letters
|May 19, 2026
PubMed
Summary
This summary is machine-generated.

Multivalent binding kinetics, unlike equilibrium, can be highly selective. This study reveals a new superselective targeting approach based on association rates, not just binding equilibrium.

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Area of Science:

  • Supramolecular chemistry
  • Chemical kinetics
  • Biophysics

Background:

  • Multivalent binding enhances avidity and selectivity over monovalent binding.
  • While equilibrium properties are understood, the nonequilibrium kinetics of multivalent interactions are not well characterized.

Purpose of the Study:

  • To systematically investigate the kinetics of multivalent binding.
  • To explore the potential for enhanced selectivity in nonequilibrium binding scenarios.
  • To develop design principles for superselective targeting.

Main Methods:

  • Experimental studies using hyaluronic acid polymers.
  • Kinetic modeling based on stochastic chemical kinetics.
  • Molecular dynamics simulations.

Main Results:

  • Both association and dissociation kinetics demonstrate greater selectivity than equilibrium binding.
  • A two-step binding model explains this phenomenon, involving fast, weak interactions followed by slow, strong ones.
  • Demonstrated a novel approach for superselective targeting utilizing association rates.

Conclusions:

  • Multivalent binding kinetics offer opportunities for enhanced selectivity beyond equilibrium considerations.
  • The findings provide a fundamental understanding of multivalent binding dynamics.
  • Established design rules for superselective targeting in dynamic systems.