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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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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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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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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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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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Self-Assembly of Structures with Addressable Complexity.

William M Jacobs1, Daan Frenkel2

  • 1Department of Chemistry and Chemical Biology, Harvard University , 12 Oxford Street, Cambridge, Massachusetts 02138, United States.

Journal of the American Chemical Society
|February 11, 2016
PubMed
Summary
This summary is machine-generated.

Predicting kinetic pathways is key for successful self-assembly of complex materials. Understanding these pathways enables the design of robust protocols for engineering novel materials with addressable complexity.

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Area of Science:

  • Materials Science
  • Chemical Engineering
  • Nanotechnology

Background:

  • Self-assembly offers a route to engineer materials with precisely defined morphologies.
  • Complex structures with hundreds of distinct building blocks have been assembled with nanometer precision.
  • Optimizing self-assembly reactions for kinetic accessibility remains a challenge.

Purpose of the Study:

  • To focus on the prediction of kinetic pathways for self-assembly.
  • To explore implications for designing robust experimental protocols.
  • To enable the engineering of complex materials using a wider range of building blocks.

Main Methods:

  • Focus on the prediction of kinetic pathways for self-assembly.
  • Analysis of factors influencing kinetic accessibility in complex self-assembly systems.
  • Development of general principles for predicting self-assembly pathways.

Main Results:

  • Recent advances demonstrate successful self-assembly of complex structures with high precision.
  • Challenges persist in ensuring kinetic accessibility of intended self-assembled structures.
  • Predicting kinetic pathways is crucial for optimizing self-assembly reactions.

Conclusions:

  • Predicting kinetic pathways is essential for robust self-assembly protocols.
  • Developing general principles will broaden the scope of building blocks for complex material engineering.
  • This work paves the way for advanced materials with addressable complexity.