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Native tertiary structure in an A-state

J L Marmorino1, M Lehti, G J Pielak

  • 1Department of Chemistry, University of North Carolina at Chapel Hill 27599-3290, USA.

Journal of Molecular Biology
|February 19, 1998
PubMed
Summary
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The A-state, a protein folding intermediate, is stabilized by a key helix-helix interaction. This interaction equally stabilizes both the A-state and the native protein structure.

Area of Science:

  • Protein folding intermediates
  • Biophysical chemistry
  • Structural biology

Background:

  • The A-state is an equilibrium species proposed as a molten globule, an on-pathway protein folding intermediate.
  • This intermediate exhibits native secondary structure but a non-native, fluctuating tertiary structure.
  • Understanding tertiary interactions in folding intermediates is crucial for deciphering protein folding pathways.

Purpose of the Study:

  • To investigate the presence and role of an evolutionary-invariant tertiary interaction within the A-state of yeast iso-1-ferricytochrome c.
  • To determine if specific tertiary interactions stabilize the A-state and the native state similarly.
  • To assess the structural characteristics of the A-state interior.

Main Methods:

  • Thermal denaturation experiments monitored by circular dichroism (CD) spectropolarimetry.

Related Experiment Videos

  • Determination of A-state and native-state stabilities (ΔG_A→D and ΔG_N→D).
  • Analysis of wild-type protein, interface variants, and control variants, along with pH and sulfate concentration dependencies.

    • Main Results:

    • A plot of A-state stability versus native-state stability for interface variants showed a slope near unity.
    • Control variants exhibited near-wild-type stability, indicating the specific role of the interface interaction.
    • The heat capacity change for A-state denaturation was approximately 60% of that for native-state denaturation.

    Conclusions:

    • The helix-helix interaction identified in the A-state significantly stabilizes both the A-state and the native state to a comparable degree.
    • The A-state interior possesses native-like characteristics, as suggested by its heat capacity change during denaturation.
    • These findings provide insights into the folding kinetics and intermediate states of ferricytochrome c.