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Related Experiment Videos

Hydrophobic effects on partial molar volume.

Takashi Imai1, Fumio Hirata

  • 1Department of Bioscience and Bioinformatics, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.

The Journal of Chemical Physics
|April 20, 2005
PubMed
Summary

Hydrophobic effects on partial molar volume (PMV) were studied. The packing effect is negative, while the iceberg effect is positive, influencing protein denaturation volume changes.

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Area of Science:

  • Physical Chemistry
  • Chemical Thermodynamics
  • Solution Chemistry

Background:

  • Hydrophobic effects are crucial in biological systems and solution chemistry.
  • Partial Molar Volume (PMV) changes provide insights into solute-solvent interactions.
  • Understanding these effects is key to comprehending protein folding and denaturation.

Purpose of the Study:

  • To investigate the hydrophobic effects on partial molar volume (PMV) during solute transfer to water.
  • To elucidate the contributions of packing and "iceberg" effects to the overall volume change.
  • To explore the influence of solute size and solvent compressibility on PMV.

Main Methods:

  • Utilized integral equation theory of liquids to model solute transfer.
  • Decomposed volume change into "packing" and "iceberg" effects.
  • Analyzed the role of solvent compressibility and solute size.

Main Results:

  • The packing effect was found to be negative, partially counteracted by a positive iceberg effect.
  • Solvent compressibility differences significantly influence the packing effect.
  • The net volume change is dependent on both solute size and solvent compressibility.

Conclusions:

  • The interplay between packing and iceberg effects dictates the PMV change.
  • Protein denaturation can lead to either an increase or decrease in protein PMV.
  • These findings have implications for understanding protein behavior under varying conditions.

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