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Related Experiment Videos

Using deeply trapped intermediates to map the cytochrome c folding landscape.

F Akif Tezcan1, William M Findley, Brian R Crane

  • 1Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 27, 2002
PubMed
Summary

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Replacing iron with cobalt(III) in cytochrome c creates a folding trap without altering protein structure or thermodynamics. This allowed detailed study of misfolded intermediates, revealing insights into protein folding pathways and conformational stability.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding Dynamics

Background:

  • Cytochrome c is a crucial heme protein involved in electron transport.
  • Understanding protein folding pathways is essential for comprehending protein function and misfolding diseases.
  • Metal ion substitution is a technique used to probe protein landscapes.

Purpose of the Study:

  • To investigate the impact of cobalt(III) substitution for iron in cytochrome c on its folding energy landscape.
  • To characterize the structure, thermodynamics, and kinetics of cobalt(III)-substituted cytochrome c folding.
  • To elucidate the nature of folding intermediates and their contribution to the overall folding process.

Main Methods:

  • Spectroscopic techniques (e.g., UV-Vis, fluorescence)

Related Experiment Videos

  • X-ray diffraction for structural analysis
  • Kinetics measurements to study folding and refolding pathways
  • Fluorescence energy-transfer analysis

    • Main Results:

    • Cobalt(III) substitution introduces a deep trap in the folding-energy landscape.
    • Protein structure and folding thermodynamics remain unperturbed by the metal-ion substitution.
    • Parallel folding pathways involving misligated Co(III) species were identified.
    • Folding intermediates persist for extended periods, allowing for detailed spectroscopic characterization.
    • Evidence suggests rapidly equilibrating compact and extended conformations coexist during refolding.

    Conclusions:

    • Metal ion substitution can selectively trap specific folding intermediates without disrupting overall protein structure.
    • The study provides direct evidence that collapsed denatured structures are not significantly more stable than extended conformations.
    • Detailed characterization of persistent folding intermediates offers new insights into protein folding dynamics.