Protein folding and unfolding under the effect of exogenous perturbations remains a topic of great interest, further enhanced by recent technological developments in the field of signal generation that allow the use of intense ultrashort electric pulses to directly interact at microscopic level with biological matter. In this paper, we show results from molecular dynamics (MD) simulations of a single myoglobin molecule in water exposed to pulsed and static electric fields, ranging from 10(8) to 10(9) V/m, compared to data with unexposed conditions. We have found that the highest intensity (10(9) V/m) produced a fast transition (occurring within a few hundreds of picoseconds) between folded and unfolded states, as inferred by secondary structures and geometrical analysis. Fields of 10(8) V/m, on the contrary, produced no significant denaturation, although a relevant effect on the protein dipolar behavior was detected.