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Related Experiment Videos

Folding of lysozyme

B Fischer1

  • 1IMMUNO AG, Biomedical Research Center, Orth an der Donau, Austria.

EXS
|January 1, 1996
PubMed
Summary
This summary is machine-generated.

Hen egg white lysozyme folding is a complex, reversible process involving distinct pathways and intermediate states. Correct disulfide bond formation is crucial for native structure and function.

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Area of Science:

  • Biochemistry
  • Protein Folding
  • Enzymology

Background:

  • Hen egg white lysozyme is a well-characterized model protein.
  • Understanding protein folding is critical in molecular biology.

Purpose of the Study:

  • To analyze the folding pathway of hen egg white lysozyme.
  • To investigate the role of disulfide bonds in lysozyme folding.

Main Methods:

  • Studied reversible unfolding and folding processes.
  • Analyzed disulfide bond formation kinetics.
  • Characterized intermediate folding states, including the molten globule.

Main Results:

  • Lysozyme folding follows cooperative and parallel pathways, with a burst-phase collapse.

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  • Secondary and tertiary structures form in distinct phases.
  • Disulfide bond formation involves nucleation and a rate-limiting step, essential for native conformation.
  • Transient molten globule states are observed during folding.

    • Conclusions:

    • Lysozyme folding is a complex, multi-phase process.
    • Disulfide bond formation is critical for achieving native structure and catalytic activity.
    • The molten globule state represents a key intermediate in the folding pathway.