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Temperature, stability, and the hydrophobic interaction

J A Schellman1

  • 1Institute of Molecular Biology, University of Oregon, Eugene 97403, USA. john@jas1.uoregon.edu

Biophysical Journal
|December 31, 1997
PubMed
Summary
This summary is machine-generated.

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The hydrophobic effect strengthens with increasing temperature, contrary to traditional understanding. Using the Massieu-Planck function (deltaG degrees/T) offers a more accurate view of temperature-dependent stability for hydrophobic interactions.

Area of Science:

  • Thermodynamics
  • Biochemistry
  • Physical Chemistry

Background:

  • Free energy changes typically assess temperature effects on protein stability and hydrophobic interactions.
  • Aqueous solubility of hydrocarbons is a standard model for the hydrophobic effect.

Purpose of the Study:

  • To re-evaluate the temperature dependence of the hydrophobic effect using thermodynamic functions.
  • To compare the utility of standard Gibbs free energy change (deltaG degrees) and the Massieu-Planck function (deltaG degrees/T) for analyzing temperature-dependent stability.

Main Methods:

  • Analysis of the aqueous solubility of hydrocarbons and protein unfolding.
  • Application of both deltaG degrees and deltaG degrees/T to interpret stability changes with temperature.

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Main Results:

  • The hydrophobic effect appears to strengthen with increasing temperature up to approximately 140°C when analyzed with standard Gibbs free energy.
  • Using the Massieu-Planck function (deltaG degrees/T) provides an alternative interpretation of temperature-dependent hydrophobic interactions.
  • Protein stability profiles show minimal changes with temperature regardless of the thermodynamic function used.

Conclusions:

  • The choice of thermodynamic function significantly impacts the interpretation of temperature effects on the hydrophobic effect.
  • The Massieu-Planck function offers a more appropriate framework for understanding temperature-dependent hydrophobic interactions.
  • Contrasting protein unfolding with nonpolar molecule hydration helps estimate other factors influencing protein structure stability.