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Related Experiment Videos

Solvent isotope effect and protein stability

G I Makhatadze1, G M Clore, A M Gronenborn

  • 1Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.

Nature Structural Biology
|October 1, 1995
PubMed
Summary
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Replacing water (H2O) with heavy water (D2O) increases protein transition temperatures but decreases unfolding enthalpy. Protein stability remains similar due to enthalpy-entropy compensation, driven by altered protein hydration in D2O.

Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Protein stability is crucial for biological function.
  • Understanding the effects of solvent isotopic composition on protein thermodynamics is important.

Purpose of the Study:

  • To comparatively study the stability of proteins in H2O and D2O.
  • To investigate the thermodynamic basis of protein stability changes in D2O.

Main Methods:

  • Differential Scanning Calorimetry (DSC) for thermal stability measurements.
  • Thermodynamic analysis of protein unfolding.
  • Thermodynamic analysis of model compound transfer between H2O and D2O.

Main Results:

  • Deuterium oxide (D2O) substitution for H2O increased protein transition temperatures.

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  • A decrease in the enthalpy of unfolding was observed in D2O.
  • Enthalpy-entropy compensation maintained overall protein stability, attributed to altered hydration.

    • Conclusions:

    • Water isotopic substitution significantly impacts protein unfolding thermodynamics.
    • Changes in protein hydration, particularly of non-polar groups, explain observed thermodynamic alterations.
    • The findings provide insights into protein-ligand interactions and hydration dynamics.