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Related Experiment Videos

Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate

G Wildegger1, T Kiefhaber

  • 1Department of Biophysical Chemistry, Biozentrum der Universität Basel,Switzerland.

Journal of Molecular Biology
|July 11, 1997
PubMed
Summary

Lysozyme folding involves two pathways, a fast direct route and a slow route via an intermediate. This intermediate, though stable, hinders folding by increasing activation energy, but doesn't alter the rate-limiting step.

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Area of Science:

  • Protein folding dynamics
  • Biophysical chemistry
  • Enzyme kinetics

Background:

  • Lysozyme folding exhibits complex kinetics with both fast and slow pathways.
  • A partially folded intermediate transiently accumulates during the slow folding pathway.

Purpose of the Study:

  • To elucidate the kinetic partitioning and mechanistic details of lysozyme folding.
  • To determine the role of the partially folded intermediate in the folding process.

Main Methods:

  • Kinetic double-jump experiments were employed to analyze folding pathways.
  • Guanidinium chloride dependencies of refolding and unfolding reactions were fitted to kinetic models.

Main Results:

  • Kinetic partitioning occurs early in refolding, directing molecules to either the direct or slow pathway.

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  • A triangular mechanism was proposed as the minimal model explaining lysozyme folding kinetics.
  • The intermediate's stability increases the free energy of activation for folding, despite identical transition state energies.

    • Conclusions:

    • The partially folded intermediate obstructs transition state formation due to pre-formed secondary structures.
    • The intermediate's presence increases the overall activation energy but does not change the rate-limiting step of lysozyme folding.