Protein folding and unfolding pathways under high pressure

Abstract

The present work focuses on the pressure induced unfolding/folding of trypsin and F31 A-Sso7. The latter protein is a hydrophobic core mutant of the extreme barostable protein Sso7d from the archaeon Suffolobus solfataricus. With respect to trypsin our results shows that the kinetics of folding and unfolding 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 theory proposed by Dill.

Key Words:

• Protein folding
• trypsin
• Sso7d