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Related Concept Videos

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...
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...
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...

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Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Complex macromolecular chimeras.

Anastasis Karatzas1, Hermis Iatrou, Nikos Hadjichristidis

  • 1Department of Chemistry, University of Athens, Panepistimiopolis, Zografou, Athens, Greece.

Biomacromolecules
|June 13, 2008
PubMed
Summary
This summary is machine-generated.

Novel polymer/polypeptide hybrids were synthesized using anionic and ring-opening polymerization. This method created complex macromolecular chimeras with high molecular weight and homogeneity.

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

Published on: January 14, 2020

Area of Science:

  • Polymer Chemistry
  • Macromolecular Science

Background:

  • Living polymerizations, including anionic and ring-opening polymerization (ROP), are crucial for synthesizing well-defined polymers.
  • Combining different polymerization techniques allows for the creation of complex polymer architectures.

Purpose of the Study:

  • To synthesize novel multiblock multicomponent linear and miktoarm star (micro-star) polymer/polypeptide hybrids (macromolecular chimeras).
  • To explore the combination of anionic polymerization and ROP for creating advanced polymer structures.

Main Methods:

  • Synthesis involved combining anionic polymerization and ROP.
  • End- or in-chain amino-functionalized polymers were synthesized via anionic polymerization under high vacuum.
  • Amino groups were utilized for the ROP of alpha-amino acid N-carboxyanhydrides (NCAs).

Main Results:

  • Successfully synthesized linear and micro-star polymer/polypeptide hybrids.
  • Molecular characterization confirmed high molecular weight and compositional homogeneity.
  • The use of high vacuum techniques for ROP of NCAs was critical for success.

Conclusions:

  • The study demonstrates a successful strategy for creating complex polymer/polypeptide hybrids.
  • High vacuum techniques are essential for controlled ROP of NCAs, preventing side reactions.
  • This approach enables the synthesis of advanced macromolecular architectures with precise control.