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Related Experiment Videos

Cytochrome c folding triggered by electron transfer

G A Mines1, T Pascher, S C Lee

  • 1Beckman Institute, California Institute of Technology, Pasadena, CA 91125 USA. winkler@bilrc.caltech.edu

Chemistry & Biology
|June 1, 1996
PubMed
Summary
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Protein folding rates are linked to free-energy changes. Horse and yeast cytochrome c proteins, despite sequence differences, exhibit similar folding pathways and rate/free-energy profiles, suggesting conserved folding mechanisms.

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Molecular Biology

Background:

  • Protein folding rates are influenced by the free-energy change of the process.
  • A novel photochemical electron-transfer-triggering method allows study of protein folding kinetics across diverse free-energy landscapes.
  • Cytochromes c from horse (h-cyt c) and yeast (y-cyt c) were chosen for their similar structures but distinct sequences and folding energies.

Purpose of the Study:

  • To investigate the relationship between protein folding rate and free-energy change.
  • To compare the folding kinetics of h-cyt c and y-cyt c using a photochemical method.
  • To elucidate the factors governing protein folding barriers.

Main Methods:

  • Utilized a photochemical electron-transfer-triggering technique to induce and monitor protein folding.

Related Experiment Videos

  • Measured folding free energies and rates for horse and yeast cytochrome c in varying concentrations of guanidine hydrochloride.
  • Analyzed the dependence of activation free energies on folding free energies.

    • Main Results:

    • Folding free energies for both proteins were linear with denaturant concentration, with y-cyt c requiring lower denaturant for unfolding.
    • When folding driving forces were matched, h-cyt c and y-cyt c displayed comparable folding rates.
    • Activation free energies for folding showed a linear dependence on folding free energies for both proteins, with similar slopes (~0.4).

    Conclusions:

    • The folding barrier height is determined by the relative stability of the folded and unfolded protein states.
    • Despite low sequence homology, horse and yeast cytochrome c follow similar folding pathways.
    • The similar rate/free-energy profiles suggest conserved folding mechanisms in these homologous proteins.