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A lysozyme folding intermediate revealed by solution X-ray scattering

L Chen1, K O Hodgson, S Doniach

  • 1Department of Chemistry, Stanford University, CA 94305, USA.

Journal of Molecular Biology
|September 6, 1996
PubMed
Summary
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This study reveals a third hen egg lysozyme species during urea-induced unfolding, identified using X-ray scattering and circular dichroism. This intermediate state offers insights into protein folding pathways.

Area of Science:

  • Biophysics
  • Protein Chemistry
  • Structural Biology

Background:

  • Hen egg lysozyme is a model protein for studying unfolding.
  • Urea is a common denaturant used to probe protein stability.
  • Understanding protein unfolding intermediates is crucial for comprehending protein folding.

Purpose of the Study:

  • To investigate the equilibrium unfolding of hen egg lysozyme using urea at pH 2.9.
  • To identify and characterize potential intermediate species during the unfolding process.
  • To correlate structural findings with thermodynamic parameters.

Main Methods:

  • Solution X-ray scattering was employed to monitor changes in protein structure.
  • Far and near UV circular dichroism (CD) spectroscopy measured secondary and tertiary structure changes.

Related Experiment Videos

  • Singular value decomposition (SVD) analysis was used to interpret scattering data.
  • The denaturant binding model was applied to determine thermodynamic parameters.

    • Main Results:

    • Differences in unfolding transitions observed via radius of gyration (Rg) and CD suggested a third species.
    • SVD analysis of X-ray scattering curves provided evidence for a third basis component.
    • Thermodynamic parameters were estimated for the intermediate and unfolded states.
    • A scattering profile for the pure intermediate state was reconstructed.

    Conclusions:

    • The study provides strong evidence for a distinct intermediate species during hen egg lysozyme unfolding.
    • The structural model of the intermediate is proposed, potentially linked to kinetic intermediates in refolding.
    • This work advances the understanding of protein folding dynamics and intermediate states.