Protein stability and dynamics in the pressure-temperature plane

Filip Meersman, László Smeller, Karel Heremans

Research output: Contribution to journalReview article

73 Citations (Scopus)


The pressure-temperature stability diagram of proteins and the underlying assumptions of the elliptical shape of the diagram are discussed. Possible extensions, such as aggregation and fibril formation, are considered. An important experimental observation is the extreme pressure stability of the mature fibrils. Molecular origins of the diagram in terms of models of the partial molar volume of a protein focus on cavities and hydration. Changes in thermal expansivity, compressibility and heat capacity in terms of fluctuations of the enthalpy and volume change of the unfolding should also focus on these parameters. It is argued that the study of water-soluble polymers might further our understanding of the stability diagram. Whereas the role of water in protein behaviour is unquestioned, the role of cavities is less clear.

Original languageEnglish
Pages (from-to)346-354
Number of pages9
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number3
Publication statusPublished - Mar 1 2006



  • Aggregation
  • Cavity
  • Hydration
  • Pressure-temperature phase diagram
  • Protein dynamics
  • Unfolding

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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