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

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.3K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.3K
Protein Complex Assembly02:41

Protein Complex Assembly

11.3K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
11.3K
Structure of Cadherins01:25

Structure of Cadherins

3.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
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...
2.6K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.0K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.0K

You might also read

Related Articles

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

Sort by
Same author

Discovery amidst Artificial Intelligence: Protein-Receptor Interactions.

Biochemistry·2026
Same author

Next Generation Hosts for Protein Recognition, Assembly and More.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Protein Recognition and Assembly by a Phosphocavitand.

Journal of the American Chemical Society·2025
Same author

N‑Terminal Protein Complexation and Assembly with a Triangular Sulfated Macrocycle.

Crystal growth & design·2025
Same author

Making and Breaking Supramolecular Synthons for Modular Protein Frameworks.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

N-Terminal Protein Binding and Disorder-to-Order Transition by a Synthetic Receptor.

Biochemistry·2025

Related Experiment Video

Updated: Sep 20, 2025

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
10:36

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

Published on: July 27, 2016

9.7K

Protein-Calixarene Complexation: From Recognition to Assembly.

Peter B Crowley1

  • 1School of Biological and Chemical Sciences, University of Galway, University Road, Galway H91 TK33, Ireland.

Accounts of Chemical Research
|June 6, 2022
PubMed
Summary

This study details advancements in protein-calixarene complexation, moving from simple recognition to creating complex frameworks. Researchers used X-ray crystallography and NMR to understand how calixarenes bind proteins, leading to new porous materials.

More Related Videos

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.4K
Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.7K

Related Experiment Videos

Last Updated: Sep 20, 2025

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
10:36

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

Published on: July 27, 2016

9.7K
In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.4K
Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.7K

Area of Science:

  • Supramolecular Chemistry
  • Biomolecular Chemistry
  • Materials Science

Background:

  • Protein-calixarene complexation has advanced significantly over the past decade.
  • Initial studies focused on binary recognition, evolving towards macrocycle-mediated frameworks.

Purpose of the Study:

  • To summarize progress in protein-calixarene complexation.
  • To highlight the evolution from molecular recognition to framework construction.
  • To encourage further research at the interface of biomolecular and synthetic chemistry.

Main Methods:

  • Cocrystallization and X-ray structure determination.
  • Solution state methods including NMR spectroscopy, isothermal titration calorimetry (ITC), and light scattering.
  • Utilized various calixarenes, including sulfonato-calix[4]arene and larger calix[n]arenes (n=6, 8).

Main Results:

  • Demonstrated calixarene encapsulation of cationic proteins like cytochrome c and Ralstonia solanacearum lectin (RSL).
  • Observed the 'bigger better binder' phenomenon with larger calixarenes, leading to increased affinities and complex assemblies.
  • Successfully designed and prepared porous molecular frameworks with high solvent content (>60%), tunable porosity dependent on protein:calixarene ratio and crystallization conditions (e.g., pH).

Conclusions:

  • Protein-calixarene complexation has evolved from simple binding to sophisticated framework construction.
  • Calixarene-based frameworks offer potential for designing novel porous molecular materials.
  • Further exploration of supramolecular protein chemistry is encouraged to drive innovation.