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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Assembly of Signaling Complexes01:30

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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.
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Protein Complexes with Interchangeable Parts01:57

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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.
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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.
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Assembly and Characterization of Polyelectrolyte Complex Micelles
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Assembly and Characterization of Polyelectrolyte Complex Micelles

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Protein-Polyelectrolyte Complexes and Micellar Assemblies.

Shang Gao1, Advait Holkar2, Samanvaya Srivastava3

  • 1Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, CA 90095, USA. gshang@ucla.edu.

Polymers
|July 3, 2019
PubMed
Summary
This summary is machine-generated.

Protein-polyelectrolyte complexes self-assemble into useful structures for applications like genetic code and targeted drug delivery. Their unique properties arise from electrostatic interactions and protein charge distribution.

Keywords:
complexationprotein deliveryself-assembly

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Area of Science:

  • Biochemistry
  • Materials Science
  • Biotechnology

Background:

  • Protein-polyelectrolyte complexes are fundamental in biological systems and biotechnological applications.
  • They play roles in genetic code, protein purification, protocellular environments, and enzymatic bioreactors.

Purpose of the Study:

  • To review recent advancements in the structure, properties, and applications of protein-polyelectrolyte complexes.
  • To explore both bulk and micellar assemblies of these complexes.

Main Methods:

  • Review of existing literature on protein-polyelectrolyte complex self-assembly.
  • Analysis of factors influencing complex formation, including electrostatic interactions and protein amphotericity.
  • Investigation of block polyelectrolyte incorporation for micellar assembly.

Main Results:

  • Protein-polyelectrolyte complexes exhibit self-assembly in bulk driven by electrostatic forces and entropy.
  • Incorporation of block polyelectrolytes leads to multifunctional protein-polyelectrolyte complex micelles for targeted delivery.
  • Unique phenomena such as multiple complexation windows and complexation beyond the isoelectric point are observed.

Conclusions:

  • Protein-polyelectrolyte complexes offer versatile platforms for diverse applications, from fundamental biological processes to advanced therapeutics.
  • Understanding their self-assembly and properties enables the design of novel functional materials.
  • Further research into charge distribution and amphoteric nature can unlock new complexation behaviors and applications.