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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Updated: Jun 13, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

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Published on: October 26, 2015

Foldamers with helical cavities for binding complementary guests.

Hemraj Juwarker1, Jae-min Suk, Kyu-Sung Jeong

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

Chemical Society Reviews
|May 8, 2010
PubMed
Summary

Foldamers, synthetic receptors formed by unnatural oligomers, create helical cavities for binding neutral molecules, cations, and anions. Their function as molecular and ionic receptors can be tuned by modular building blocks.

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Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry
  • Bioorganic Chemistry

Background:

  • Foldamers are synthetic receptors utilizing unnatural oligomers.
  • They form helical cavities through noncovalent interactions, not covalent bonds.
  • Functional groups arrange within these cavities for guest complexation.

Purpose of the Study:

  • To introduce helical cavities formed by foldamers.
  • To summarize the binding of neutral molecules, cations, and anions within these cavities.
  • To highlight foldamers as emerging synthetic receptors.

Main Methods:

  • Review of foldamer chemistry and supramolecular binding principles.
  • Analysis of noncovalent interactions driving foldamer folding.
  • Discussion of modular building blocks for receptor tuning.

Main Results:

  • Foldamers effectively bind neutral molecules, cations, and anions.
  • Helical cavity formation is driven by noncovalent interactions.
  • Tuning of binding properties is achievable through foldamer design.

Conclusions:

  • Foldamers represent a versatile platform for synthetic receptor design.
  • Their ability to form tunable helical cavities enables molecular and ionic recognition.
  • This review serves as an introduction for researchers in supramolecular, organic, and bioorganic chemistry.