Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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,...

Protein-protein Interfaces

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: Ligands

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...

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...

You might also read

Related Articles

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

Sort by

Same author

A tetrahedron from homooxacalix[3]arene, the fifth Platonic polyhedron from calixarenes and uranyl.

Frontiers in chemistry·2023

Same author

Metal Coordination Guided Formation of Discrete Neutral Three-Component Hydrogen-Bonded Architectures.

Organic letters·2020

Same author

Selective Formation of <i>S</i><sub>4</sub>- and <i>T</i>-Symmetric Supramolecular Tetrahedral Cages and Helicates in Polar Media Assembled via Cooperative Action of Coordination and Hydrogen Bonds.

Journal of the American Chemical Society·2020

Same author

A Synthetic Cation-Transporting Calix[4]arene Derivative Active in Phospholipid Bilayers.

Angewandte Chemie (International ed. in English)·2018

Same author

A Self-Assembled Calix[4]arene Dimer Linked through Hydrogen-Bonded 2-Ureidopyrimidin-4(1H)-one Groups.

Angewandte Chemie (International ed. in English)·2018

Same author

Molecular Basis for the Recognition of Higher Fullerenes into Ureidopyrimidinone-Cyclotriveratrylene Self-Assembled Capsules.

Chemistry (Weinheim an der Bergstrasse, Germany)·2016

Search research articles

Related Experiment Video

Updated: May 13, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Dynamic multivalency for carbohydrate-protein recognition through dynamic combinatorial libraries based on

Philipp Reeh¹, Javier de Mendoza

¹The Institute of Chemical Research of Catalonia (ICIQ), Avda. Països Catalans 16, 43007-Tarragona, Spain.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|March 16, 2013

Summary

This summary is machine-generated.

Dynamic combinatorial libraries (DCLs) using iron complexes enhance carbohydrate-protein binding. This method shows a preference for mannose-containing molecules when interacting with concanavalin A (ConA).

More Related Videos

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Related Experiment Videos

Last Updated: May 13, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

Biochemistry
Chemical Biology
Molecular Recognition

Background:

Carbohydrate-protein interactions are crucial in biological processes.
Dynamic combinatorial libraries (DCLs) offer a powerful approach for discovering molecular binders.
Multivalency and metal coordination can significantly enhance molecular recognition.

Purpose of the Study:

To investigate the use of a DCL system for carbohydrate-protein recognition.
To explore the impact of multivalency and metal coordination on binding affinity.
To identify specific carbohydrate-binding preferences of concanavalin A (ConA).

Main Methods:

Construction of a three-component DCL based on 2,2'-bipyridine (bipy)-Fe(II) complexes.
Testing the DCL's interaction with concanavalin A (ConA).
Analysis of binding affinities and selectivity using multivalent presentation.

Main Results:

The DCL demonstrated enhanced binding to ConA through multivalent presentation.
A clear bias was observed towards mannose-containing components within the library.
Metal coordination (Fe(II)) played a key role in the DCL's recognition capabilities.

Conclusions:

DCLs exploiting metal coordination and multivalency are effective for carbohydrate-protein recognition.
This approach can be tailored to achieve selective binding, as shown with mannose and ConA.
The findings provide insights into designing molecular probes for specific biological targets.