Protein folding and unfolding pathways under high pressure

The present work focuses on the pressure induced unfolding/folding of tryps in and F31A-Sso7. The latter protein is a hydrophobic core mutant of the ex treme barostable protein Sso7d from the archaeon Sulfolobus solfataricus. W ith respect to trypsin our results shows that the kinetics of folding and u nfolding are different. On the other hand the experiments carried out with F31A-Sso7d suggest that the protein can exist in two native conformational states. These results point out that the folding process can be complex and that such a complexity can be fully described by the energy landscape theo ry proposed by Dill.