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Revisiting the Anfinsen cage

Ellis1

  • 1R John Ellis, Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.

Folding & Design
|January 1, 1995
PubMed
Summary

Chaperonin experiments reveal protein folding is not spontaneous but involves molecular chaperones. These ATPases enhance folding efficiency within crowded cells, preventing unproductive interactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Recent experiments with chaperonins have reshaped understanding of intracellular protein folding.
  • Protein folding was previously considered a spontaneous, energy-independent process.

Purpose of the Study:

  • To review a model for chaperonin function in protein folding.
  • To discuss the role of chaperonins in the crowded cellular environment.

Main Methods:

  • Review of experimental findings on chaperonin family molecular chaperones.
  • Historical context analysis of protein folding models.

Main Results:

  • Protein folding efficiency is increased by transient interactions with chaperonin ATPases.
  • Chaperonins act as "Anfinsen cages" to prevent and reverse unproductive protein interactions.

Conclusions:

  • Intracellular protein folding is an assisted process, not purely spontaneous.
  • Chaperonins are crucial for efficient and correct protein folding within cells.

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