Abstract
The nature of the pressure-unfolded state of a protein is still under debate. Since high pressure favours states with lower molar volume, the pressure-unfolded state is often thought to be more compact than a random coil. However, differences between effect of pressure and other unfolding methods might often reflect the fact that pressure acts locally on the protein structure and hence differentially destabilizes different domains of a protein. The unfolded state of I98A mutant of the C-terminal domain of L9 protein has been studied by pH, urea denaturation and also cold temperature, since the protein undergoes cold denaturation above 0°C.
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