Abstract
Proteins are subjected to electric fields both within the cell and during routine biochemical analysis. We have used atomistic molecular dynamics simulations to study conformational changes within three structurally diverse proteins subjected to high electric fields. At electric fields in excess of .5 V/nm, major structural changes were observed in all three proteins due to charge redistribution within the biomolecule. However, the electromechanical resilience was found to be highly dependent on the protein secondary structure, with α-helices showing a particularly high susceptibility to deformation by the applied electric field.
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Acknowledgements
We acknowledge Al-Azhar University, Egypt, for providing studentship funding for AAAE. We are very grateful to Peter Olmsted, Peter Winlove and Phil Fowler for careful reading of the manuscript and for the helpful suggestions that they made.