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Related Concept Videos

Protein Folding01:25

Protein Folding

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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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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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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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Related Experiment Video

Updated: Apr 25, 2026

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

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To assemble or fold?

Anindita Das1, Suhrit Ghosh

  • 1Indian Association for the Cultivation of Science, Polymer Science Unit, Kolkata-700032, India. psusg2@iacs.res.in.

Chemical Communications (Cambridge, England)
|August 21, 2014
PubMed
Summary

This study reveals how a donor-acceptor dyad self-assembles into complex structures. Through folding and hydrogen bonding, it forms a folded dimer that further organizes into reverse-vesicles.

Area of Science:

  • Supramolecular chemistry
  • Materials science

Background:

  • Donor-acceptor (D-A) dyads are fundamental building blocks in supramolecular chemistry.
  • Controlling self-assembly is crucial for designing advanced functional materials.

Purpose of the Study:

  • To investigate the stepwise folding and assembly of an amide functionalized D-A dyad.
  • To elucidate the mechanism of macroscopic structure formation from molecular components.

Main Methods:

  • Synthesis of an amide functionalized D-A dyad.
  • Characterization of molecular conformation and intermolecular interactions (e.g., CT-interaction, H-bonding).
  • Analysis of self-assembly processes in solution (MCH) and resulting macroscopic structures.

Main Results:

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  • The D-A dyad adopts a folded conformation driven by intra-chain charge-transfer (CT) interaction.
  • Intermolecular hydrogen bonding leads to the formation of a folded dimer (FD) with a specific DAAD stacking.
  • Solvophobic effects and pi-stacking drive the assembly of FDs into reverse-vesicles.

Conclusions:

  • Demonstrates a rational design for stepwise self-assembly from molecular dyads to macroscopic structures.
  • Highlights the interplay of intramolecular and intermolecular forces in dictating self-assembly pathways.
  • Reports the formation of novel reverse-vesicle structures through a multi-stage assembly process.