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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Protein Complexes with Interchangeable Parts01:57

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...

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

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Macromolecular assemblies based on coupled inclusion complex and electrostatic interactions.

Virginie Burckbuchler1, Valérie Boutant, Véronique Wintgens

  • 1Laboratoire de Recherche sur les Polymères, LRP, C.N.R.S. UMR 7581, 2-8 rue Henri Dunant, 94320 Thiais, France.

Biomacromolecules
|October 10, 2006
PubMed
Summary

Researchers created macromolecular assemblies using polymers and amphiphiles. Increasing cation concentration led to larger aggregates, with counterion type influencing size and compactness.

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Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
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Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Area of Science:

  • Supramolecular Chemistry
  • Polymer Science
  • Materials Science

Background:

  • Macromolecular assemblies are crucial in various scientific fields.
  • Understanding their formation and properties is key for developing new materials.

Purpose of the Study:

  • To investigate the formation and structural properties of ternary macromolecular assemblies.
  • To explore the influence of component concentration and counterion nature on aggregate structure.

Main Methods:

  • Viscometry
  • Small-angle neutron scattering (SANS)
  • Synthesis of beta-cyclodextrin-containing polymers (polybetaCD), dextran sulfate polyanion (NaDxS), and cationic adamantane derivatives (Ada1, Ada2).

Main Results:

  • Ternary aggregates formed via inclusion complex and electrostatic interactions.
  • Increased cation concentration resulted in larger, less compact aggregates, leading to phase separation.
  • A core-shell association mechanism was proposed: polybetaCD core, NaDxS shell, with Ada amphiphiles in cavities.
  • Counterion type significantly affected aggregate structure (e.g., Ada1/I(-) vs. Ada2/Br(-)).

Conclusions:

  • The study elucidates the self-assembly mechanism of polybetaCD/NaDxS/Ada systems.
  • Concentration and counterion identity are critical parameters controlling aggregate morphology.
  • The findings provide insights into designing functional supramolecular materials.