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

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.

Key Words:

• Pressure
• protein folding
• metmyoglobin