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Related Concept Videos

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...
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.
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Drug-Receptor Bonds01:25

Drug-Receptor Bonds

Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
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Ion Exchange01:17

Ion Exchange

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Related Experiment Video

Updated: Jun 6, 2026

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Multibody effects in ion binding and selectivity.

Sameer Varma1, Susan B Rempe

  • 1Biological and Material Sciences Center, Sandia National Laboratories, Albuquerque, NM, USA. svarma@iit.edu

Biophysical Journal
|November 18, 2010
PubMed
Summary
This summary is machine-generated.

Electronic polarization significantly impacts ion binding to biomolecules, influencing affinities and distinguishing ions like sodium (Na+) and potassium (K+). These multibody effects are crucial for understanding complex ion-ligand interactions.

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay
10:41

Capturing the Interaction Kinetics of an Ion Channel Protein with Small Molecules by the Bio-layer Interferometry Assay

Published on: March 7, 2018

Area of Science:

  • Computational Chemistry
  • Biophysics
  • Biomolecular Simulations

Background:

  • Selective ion binding is fundamental to biological processes.
  • Understanding ion-ligand interactions requires accounting for induced electronic effects.

Purpose of the Study:

  • To investigate the role of electronic polarization in selective ion binding.
  • To study sodium (Na+) and potassium (K+) binding to biomolecule functional groups.

Main Methods:

  • Quantum chemical simulations.
  • Pairwise-additive force-field simulations.
  • Studied Na+ and K+ binding to representative small molecules.

Main Results:

  • Electronic polarization significantly affects absolute and relative ion-binding affinities.
  • Multibody interactions influence molecular dipole moments and ion coordination.
  • Differential polarization aids in thermodynamically distinguishing Na+ and K+.

Conclusions:

  • Electronic polarization is a critical factor in ion-ligand interactions and selectivity.
  • Multibody effects are essential for accurately modeling ion binding thermodynamics.
  • Polarization likely plays a key role in distinguishing various ions and functional groups.