In this paper we present a general theoretical-computational approach to model the protein unfolding thermodynamics response to intense electric fields. The method proposed, based on atomistic simulations requiring limited computational effort, seems very promising to predict the unfolding thermodynamics field dependence, shedding light on the mechanisms involved. Application to myoglobin indicates a well defined field interval for a significant unfolding-refolding equilibrium with a melting field intensity ranging from 5.5 x 10(7) to 6.0 x 107 V m(-1) according to the protein-solvent system geometrical shape, suggesting a similar behaviour for other globular proteins.
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