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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.
Protein Structure Is Critical to Its Biological Function
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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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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
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Fibrous Proteins00:55

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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

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Folding and Characterization of a Bio-responsive Robot from DNA Origami
07:59

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Synthetic foldamers.

Gilles Guichard1, Ivan Huc

  • 1European Institute of Chemistry and Biology, University of Bordeaux-CNRS UMR 5248, 2 rue Escarpit, 33607 Pessac, France. g.guichard@iecb.u-bordeaux.fr

Chemical Communications (Cambridge, England)
|April 13, 2011
PubMed
Summary
This summary is machine-generated.

Foldamers are synthetic molecules mimicking biopolymers. Chemical synthesis advances enable complex, protein-like structures for new applications in medicine and materials science.

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Area of Science:

  • Synthetic chemistry
  • Supramolecular chemistry
  • Biomaterials science

Background:

  • Foldamers are artificial molecular architectures inspired by biopolymers.
  • Recent progress involves chemical synthesis of novel foldameric structures.
  • These structures offer new self-organized molecular scaffolds.

Purpose of the Study:

  • To highlight recent developments in chemically synthesized foldamers.
  • To discuss the potential of these novel molecular scaffolds.
  • To explore applications of foldamers in various scientific fields.

Main Methods:

  • Chemical synthesis of foldamers.
  • Characterization of foldamer structures and properties.
  • Exploration of foldamer self-organization.

Main Results:

  • Development of synthetic objects with protein-like size and complexity.
  • Creation of foldamers lacking alpha-amino acids.
  • Demonstration of foldamers as versatile molecular building blocks.

Conclusions:

  • Foldamers represent a significant advancement in synthetic molecular design.
  • Chemically synthesized foldamers offer new tools for creating biologically active substances, synthetic receptors, and novel materials.
  • The field provides exciting perspectives for future innovations in molecular science.