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Nonideality and protein thermal denaturation.

J C Waldner1, S J Lahr, M H Edgell

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

Biopolymers
|April 8, 1999
PubMed
Summary
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The thermal denaturation of eglin c protein is concentration-dependent due to nonideal solution behavior, not aggregation or intermediates. This finding explains discrepancies in denaturation enthalpy measurements for other proteins.

Area of Science:

  • Biochemistry
  • Biophysical Chemistry
  • Protein Chemistry

Background:

  • Protein thermal denaturation is often modeled using a two-state system.
  • Concentration-dependent changes in denaturation thermodynamics can indicate aggregation or intermediates.
  • Eglin c is a small, heat-stable proteinase inhibitor.

Purpose of the Study:

  • To investigate the concentration-dependent thermal denaturation of eglin c.
  • To determine the underlying cause of observed thermodynamic anomalies at higher protein concentrations.
  • To reconcile discrepancies between calorimetric and van't Hoff denaturation enthalpies.

Main Methods:

  • Circular Dichroism (CD) spectropolarimetry to monitor protein structure changes during denaturation.
  • Differential Scanning Calorimetry (DSC) to measure heat absorption during thermal transitions.

Related Experiment Videos

  • Analytical Ultracentrifugation (AUC) to assess protein solution behavior and aggregation state.

    • Main Results:

    • At low concentrations, eglin c denaturation followed a two-state model.
    • At higher concentrations, calorimetric enthalpy and transition temperature increased with protein concentration.
    • AUC data confirmed eglin c is monomeric but exhibited nonideal solution behavior, explained by a second virial coefficient.
    • DSC data were consistent with nonideal solution behavior, not aggregation or intermediates.

    Conclusions:

    • The concentration dependence of eglin c thermal denaturation arises from differential nonideality between the native and denatured states.
    • This nonideality is attributed to the protein's high charge at acidic pH and is influenced by buffer concentration.
    • The findings provide a potential explanation for differing van't Hoff and calorimetric denaturation enthalpies in other proteins exhibiting two-state behavior.