Pressure-assisted cold unfolding of proteins and its effects on the conformational stability compared to pressure and heat unfolding

F. Meersman, L. Smeller, K. Heremans

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The pressure-assisted cold unfolding of metmyoglobin was investigated and the cold unfolded state was compared to the heat and pressure unfolded states. Conformationally and mechanistically the pressure and cold unfolding processes are found to be very alike, while the heat unfolding shows some pronounced differences. We also propose a hypothesis on protein aggregation.

Original languageEnglish
Pages (from-to)263-268
Number of pages6
JournalHigh Pressure Research
Volume19
Issue number1-6
Publication statusPublished - 2000

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proteins
heat

Keywords

  • Metmyoglobin
  • Pressure
  • Protein folding

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Pressure-assisted cold unfolding of proteins and its effects on the conformational stability compared to pressure and heat unfolding. / Meersman, F.; Smeller, L.; Heremans, K.

In: High Pressure Research, Vol. 19, No. 1-6, 2000, p. 263-268.

Research output: Contribution to journalArticle

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