Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
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...
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...
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.
In...
Complexation Equilibria: Overview01:23

Complexation Equilibria: Overview

Complexation reactions take place when dative or coordinate covalent bonds form between metal ions and ligands. The compounds formed in these reactions are called coordination compounds. The number of bonds formed between the metal ion and the ligands is called its coordination number. Generally, most metal ions in an aqueous solution are solvated by water molecules and thus exist as aqua complexes.
The equilibrium constant of the complexation reaction is represented as the formation constant...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structural rewiring of IL-7R dimerization by an oncogenic transmembrane mutation can be reversed by rational design.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Phospholipid-driven conformational switching of HCV NS5A links protein folding to replication membrane remodeling.

Science advances·2026
Same author

Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.

Nature communications·2026
Same author

A Modular Toolkit for Nanoscale Interrogation of Multiprotein Assemblies Inside Living Cells.

ACS nano·2026
Same author

Hour-scale single-molecule imaging reveals dynamic assembly of the Wnt co-receptors LRP6 and ROR2 into common signalosomes.

Science signaling·2026
Same author

Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.

Journal of chemical theory and computation·2026
Same journal

Reaction Optimization for Enzymatic Deconstruction of Industrially Relevant Nylon Composites.

Chembiochem : a European journal of chemical biology·2026
Same journal

Deploying Artificial Metalloenzymes in Complex Environments: Strategies and Applications.

Chembiochem : a European journal of chemical biology·2026
Same journal

Synthetic Ligands of Myeloid C-Type Lectin Receptors.

Chembiochem : a European journal of chemical biology·2026
Same journal

Vancomycin-Mediated Binding of DNA Origami Nanostructures to Gram-Positive and Gram-Negative Bacteria.

Chembiochem : a European journal of chemical biology·2026
Same journal

Mutasynthesis and Antibiotic Activity of Mupirocin Analogues.

Chembiochem : a European journal of chemical biology·2026
Same journal

Pressure-Dependent Aromatic Ring Flips Reveal Variable Transition-State Volume and Compressibility Among Structural Regions of BPTI.

Chembiochem : a European journal of chemical biology·2026
See all related articles

Related Experiment Video

Updated: Jun 22, 2026

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

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

Published on: November 2, 2011

Selectivity of competitive multivalent interactions at interfaces.

Thomas André1, Annett Reichel, Karl-Heinz Wiesmüller

  • 1Department of Molecular Biology, Interfaculty Institute for Cell Biology, University of Tübingen, Auf der Morgenstelle 15, 72076 Tübingen, Germany.

Chembiochem : a European Journal of Chemical Biology
|July 1, 2009
PubMed
Summary
This summary is machine-generated.

Synthetic ligands controlling biomolecular interactions are challenging. Multivalent chelator headgroups (MCHs) enhance binding affinity and selectivity for oligohistidine peptides, crucial for controlled molecular recognition at interfaces.

More Related Videos

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
14:43

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

Published on: September 23, 2013

Related Experiment Videos

Last Updated: Jun 22, 2026

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
13:22

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

Published on: November 2, 2011

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions
12:30

Avidity-based Extracellular Interaction Screening (AVEXIS) for the Scalable Detection of Low-affinity Extracellular Receptor-Ligand Interactions

Published on: March 5, 2012

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications
14:43

Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

Published on: September 23, 2013

Area of Science:

  • Biomolecular interactions
  • Synthetic chemistry
  • Surface science

Background:

  • Developing synthetic ligands for precise biomolecular interaction control is a significant challenge.
  • Oligohistidine peptides binding to nickel-loaded nitrilotriacetic acid (NTA) is a well-established recognition system.
  • Multivalent chelator headgroups (MCHs) significantly enhance binding affinities compared to monovalent systems.

Purpose of the Study:

  • To investigate the selectivity of different oligohistidine peptides binding to immobilized MCHs.
  • To explore how varying multivalency affects binding affinity and discrimination between peptides.
  • To understand the role of surface multivalency in controlling molecular recognition at interfaces.

Main Methods:

  • Utilized microarrays of NTA chelators (mono-, bis-, tris-, tetrakis-) at varying surface densities.
  • Tested discrimination between fluorescently labeled hexahistidine and decahistidine peptides.
  • Employed kinetic binding assays using dual-color total internal reflection fluorescence spectroscopy.

Main Results:

  • Ligand discrimination showed minimal dependence on chelator type or density when peptides were tested individually.
  • Co-incubation revealed decreased affinity for hexahistidine and increased affinity for decahistidine.
  • Decahistidine binding became highly dependent on MCH density, with evidence of His6 being actively exchanged by His10.

Conclusions:

  • Surface multivalency is critical for achieving selectivity in multivalent interactions at interfaces.
  • The density of MCHs plays a key role in discriminating between different oligohistidine peptides.
  • This system offers a powerful method for tuning binding affinities and achieving specific molecular recognition.