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The structural response of chignolin to 1 V/nm electric fields of different frequencies has been studied with molecular dynamics simulations and stochastic modeling. It was found that oscillating electric fields induce conformational changes to chignolin that are frequency dependent. For frequencies comparable with or smaller from the orientational self-diffusion rate, the peptide destabilizes after performing an oscillatory motion between the two possible directions of the electric field axis. For higher frequencies the field effects are averaged out and chignolin performs a Brownian rotation diffusion maintaining its native conformation. Stochastic modeling can describe chignolin’s oscillatory motion equally well with the molecular dynamics simulations. The time needed for these changes to take place has a stochastic nature depending, beyond frequency, on factors related with the hydrogen bonds’ stability and their geometrical arrangement in the structure.

The effect of homogeneous and constant external electric fields on the structural stability of chignolin, a typical β-hairpin peptide, has been studied for 10ns using molecular dynamics simulations. The peptide aligns quickly its total dipole moment with the external electric field and then a constant stress is applied on its charged residues. For weaker fields this has mixed effects on the creation, destruction or strength of hydrogen bonds, but ultimately for strong fields chignolin unfolds starting by the separation of the terminal residues. Since the function of proteins is critically linked to their three-dimensional structures, these findings indicate that exposure to external electric fields may induce changes in conformation that can potentially initiate severe cellular dysfunction.