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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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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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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...
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Updated: Oct 23, 2025

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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Protein Assembly by Design.

Jie Zhu1, Nicole Avakyan1, Albert Kakkis1

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0340, United States.

Chemical Reviews
|August 18, 2021
PubMed
Summary
This summary is machine-generated.

Scientists are designing artificial protein assemblies with novel structures and functions by combining various scientific disciplines. This review covers strategies, structures, and properties of these advanced protein-based materials.

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Area of Science:

  • Biophysics
  • Supramolecular Chemistry
  • Materials Science
  • Protein Engineering

Background:

  • Proteins serve as fundamental building blocks for natural molecular machines and materials.
  • Natural protein assemblies inspire the rational design of artificial counterparts.
  • Controlling the self-assembly of complex proteins requires interdisciplinary approaches.

Purpose of the Study:

  • To provide an overview of the interdisciplinary field of artificial protein assemblies.
  • To outline design strategies and tools for controlling protein self-assembly.
  • To describe the structures and highlight the emergent properties of artificial protein assemblies.

Main Methods:

  • Integration of experimental and computational biophysics.
  • Application of principles from supramolecular, inorganic, materials, and polymer chemistry.
  • Development of creative strategies for controlling protein self-assembly.

Main Results:

  • Significant advancements in creating artificial protein assemblies with unprecedented structures and functions.
  • Emergence of protein-based materials with unique and unusual properties.
  • Demonstration of successful control over protein self-assembly through innovative strategies.

Conclusions:

  • The field of artificial protein assemblies has rapidly evolved over the past two decades.
  • Interdisciplinary research has led to novel protein-based structures and materials.
  • Continued exploration promises further breakthroughs in protein engineering and materials science.