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The barriers in protein folding

T R Sosnick1, L Mayne, R Hiller

  • 1Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania, Philadelphia 19104-6059, USA.

Nature Structural Biology
|March 1, 1994
PubMed
Summary
This summary is machine-generated.

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Protein folding can be rapid by eliminating specific interactions in denatured cytochrome c, bypassing slow intermediates. This challenges the idea that protein folding steps are inherently slow, suggesting barriers are optional.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Dynamics

Background:

  • Protein folding is crucial for biological function.
  • The process is often thought to involve slow, rate-limiting steps.
  • Cytochrome c folding has been a model system for studying these processes.

Purpose of the Study:

  • To investigate the folding kinetics of cytochrome c.
  • To identify and eliminate barriers in the protein folding pathway.
  • To challenge existing models of protein folding rates.

Main Methods:

  • Studying the folding of denatured cytochrome c.
  • Utilizing kinetic measurements on a millisecond timescale.
  • Analyzing the role of specific intermolecular interactions during folding.

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Main Results:

  • Eliminating a specific interaction in denatured cytochrome c allowed rapid folding (15 ms) to the native state.
  • Observable intermediates were not populated during this rapid folding.
  • This contradicts the notion that the molten globule to native state transition is intrinsically slow.

Conclusions:

  • Protein folding intermediates may be kinetically trapped by optional barriers, not integral ones.
  • The initial chain condensation step can introduce major folding barriers.
  • Protein folding can be significantly faster than previously assumed.