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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.
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Meersman et al. (2000) studied this question.
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