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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

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Origami Inspired Self-assembly of Patterned and Reconfigurable Particles
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Published on: February 4, 2013

Sheet-forming abiotic hetero foldamers.

Pranjal K Baruah1, Naduthottiyil K Sreedevi, Baisakhi Majumdar

  • 1Division of Organic Synthesis, National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India.

Chemical Communications (Cambridge, England)
|May 16, 2008
PubMed
Summary

Researchers report novel abiotic hetero oligomers with a defined sheet-like structure. These self-assembled structures are formed from repeating constrained amino acid residues, offering new possibilities in materials science.

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Fabrication of Three-Dimensional Graphene-Based Polyhedrons via Origami-Like Self-Folding

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Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Polymer Chemistry

Background:

  • Self-assembly is a fundamental process in nature and materials science.
  • Oligomers offer tunable properties based on their sequence and structure.
  • Abiotic synthesis of complex molecular architectures remains a challenge.

Purpose of the Study:

  • To report the synthesis and structural characterization of novel abiotic hetero oligomers.
  • To investigate the self-assembly behavior of these oligomers into extended structures.
  • To explore the potential of conformationally constrained amino acid residues in directing self-assembly.

Main Methods:

  • Synthesis of conformationally constrained aliphatic and aromatic amino acid monomers.
  • Polymerization to form hetero oligomers with regular repeating sequences.
  • Characterization of oligomer structure using techniques such as NMR and X-ray diffraction.
  • Analysis of self-assembly into sheet-like structures via microscopy and scattering methods.

Main Results:

  • Successful synthesis of abiotic hetero oligomers with precisely controlled sequences.
  • Observation of well-defined, extended self-assembled sheet-like structures.
  • Demonstration that conformationally constrained residues dictate the assembly pathway.
  • Structural analysis confirmed the proposed sheet-like architecture.

Conclusions:

  • Abiotic hetero oligomers can form ordered, extended self-assembled structures.
  • Conformationally constrained amino acid residues are key building blocks for directed self-assembly.
  • These findings open avenues for designing novel functional materials based on abiotic self-assembly principles.