Pressure induced changes have been investigated in both protein structure and activity. Structural changes were assessed by equilibrium and kinetic methods using pressure in situ, applied to several model proteins. For prion proteins (including URE 2 from yeast) and ataxine, a combination of extreme conditions of temperature and pressure was shown to modulate selectively the pathways of protein unfolding, aggregation, and fibril formation. In the case of mammalian prions this led to reproduce in vitro a protein structure which had all the characteristics of the pathogenic scrapie form. Pressure-jump experiments with Ribonuclease A and three proteins from plant photo-system II revealed complex protein folding and unfolding pathways. This suggested folding mechanisms involving high-dimensional energy-surfaces. Heat-shock proteins were used to study the mechanism of formation and pressure-induced dissociation of very large oligomers. Protein activity was assessed by studying enzyme activity and individual reaction steps of butyl-cholinesterase, cytochrome P450 and a carboxypeptidase from the thermophilic archaebacteria Sulfolobus solfataricus. The results inform about the relative importance of electrostatic and hydrophobic interactions in elementary steps of enzyme catalysed complex reactions. These data are essential for a better understanding of enzyme activity and may reveal useful in medical or biotechnological applications.

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