Pressure unfolding facilitates the formation of temperature gels

László Smeller, Peter Rubens, Karel Heremans

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3 Citations (Scopus)


The formation of protein aggregates after pressure treatment was investigated by Fourier Transform Infrared Spectroscopy (FTIR). The results show that the pressure unfolded protein ends in a conformation, after the release of the pressure, which has an increased tendency to aggregate, even at temperatures lower than the denaturation temperature of the untreated protein. After pressure pretreatment the infrared spectrum shows the same intermolecular antiparallel β-structure features as observed after a temperature treatment that gives rise to protein gelation. On the other hand, this structure can be destabilized by applying moderate pressures, which are significantly lower than the corresponding denaturation pressure.

Original languageEnglish
Pages (from-to)323-329
Number of pages7
JournalHigh Pressure Research
Issue number1-6
Publication statusPublished - Jan 1 2000



  • Aggregation
  • Gelation
  • Myoglobin
  • Pressure
  • Protein
  • Unfolding

ASJC Scopus subject areas

  • Condensed Matter Physics

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