Cold Inactivation of Proteins

The parabolic nature of the thermal stability profile, which for obvious reasons terminates at the freezing point of water, led Brandts to 

Perhaps the most important results obtained from undercooling studies on proteins can be summarised as follows  

Cold denaturation (unfolding, dissociation, inactivation) is 100% reversible, even at high protein concentrations. 

The mechanism of cold inactivation in undercooled water differs from that brought about by cryosolvents. 

In its cold-inactivated state, a protein is not markedly susceptible to pH changes or salt effects and is not subject to aggregation. 

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