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Intermediate states in protein folding

P L Privalov1

  • 1Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.

Journal of Molecular Biology
|May 24, 1996
PubMed
Summary

Protein folding is rapid, with transient, unstable intermediates. Stable partly folded states are typically misfolded or retain a specific, structured domain.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein folding efficiency suggests intermediate states.
  • Partly folded stable states are often misfolded or partially unfolded.
  • A retained folded subpart can act as a protein domain.

Purpose of the Study:

  • To analyze the nature of partly folded stable protein states.
  • To investigate the characteristics of retained folded subparts in proteins.
  • To understand the kinetics of protein folding for small single-domain proteins.

Main Methods:

  • Critical analysis of experimental data on partly folded proteins.
  • Fragmentation to isolate retained folded subparts.
  • Observation of unfolding/refolding experiments.

Main Results:

  • Stable partly folded states are either misfolded or retain a structured domain.
  • This retained domain possesses a definite tertiary structure maintained by long-range interactions.
  • Small single-domain proteins fold rapidly if not trapped in misfolded forms.

Conclusions:

  • Partly folded stable states are not true folding intermediates but rather misfolded forms or intact domains.
  • The retained folded subpart can be considered a distinct protein domain.
  • Protein folding intermediates are transient and highly unstable.

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