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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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Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Molecular Chaperones and Protein Folding03:00

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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

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.
The...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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Origami Inspired Self-assembly of Patterned and Reconfigurable Particles
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Anion-controlled foldamers.

Hemraj Juwarker1, Kyu-Sung Jeong

  • 1Center for Bioactive Molecular Hybrids, Department of Chemistry, Yonsei University, 134, Shinchon, Seoul, Republic of Korea.

Chemical Society Reviews
|August 24, 2010
PubMed
Summary

Anions direct the folding and secondary structures of synthetic oligomers and polymers. This anion-mediated process also modulates molecular recognition and physical properties in these macromolecules.

Area of Science:

  • Supramolecular Chemistry
  • Polymer Science
  • Organic Chemistry

Background:

  • Anions are increasingly important in supramolecular chemistry.
  • Synthetic oligomers and polymers can be designed for anion recognition.

Purpose of the Study:

  • To review the role of anions in directing the folding and secondary structures of synthetic oligomers and polymers.
  • To summarize anion-responsive behaviors and their impact on physical properties.

Main Methods:

  • Review of existing literature on anion-mediated folding.
  • Analysis of supramolecular architectures designed with hydrogen bond donors.
  • Examination of anion binding within cavities of foldamers, macrocycles, and polymers.

Main Results:

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  • Anion binding induces folding and helical structures in linear and cyclic oligomers.
  • Anions modulate the secondary structures and physical properties of polymers.
  • Hydrogen bond donors are key for complementary anion recognition.

Conclusions:

  • Anion-mediated processes offer precise control over macromolecular structure and function.
  • This review highlights the versatility of anions in supramolecular design.
  • Future research can leverage anion-responsive systems for advanced materials.