Resistance of biomolecules to high electric fields is a main concern for nanobioelectronics/nanobiosensing applications, and it is also a relevant issue from a fundamental perspective, to understand the dielectric properties and structural dynamics of proteins. In nanoscale devices, biomolecules may experience electric fields as high as 107 V/m in order to elicit charge transport/transfer. Understanding the effects of such fields on their structural integrity is thus crucial to assess the reliability of biomolecular devices. In this study, we show experimental evidence for the retention of native-like fold pattern by proteins embedded in high electric fields. We have tested the metalloprotein azurin, deposited onto SiO2 substrates in air with proper electrode configuration, by applying high static electric fields (up to 106-107 V/m). The effects on the conformational properties of protein molecules have been determined by means of intrinsic fluorescence measurements. Experimental results indicate that no significant field-induced conformational alteration occurs. This behavior is also discussed and supported by theoretical predictions of the intrinsic intra-protein electric fields. As the general features of such inner fields are not peculiar of azurin, the conclusions presented here should have general validity.