title: A comparison of the electromechanical properties of structurally diverse proteins by molecular dynamics simulation.
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.
authors.affiliation: a School of Physics and Astronomy, University of Leeds , Leeds , UK .
authors.forename: Asmaa A A
authors.initials: AA
authors.lastname: Elsheshiny
authors.forename: Alison E
authors.initials: AE
authors.lastname: Ashcroft
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Harris
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry*; D004560:Electricity; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D055595:Mechanical Phenomena; D056004:Molecular Dynamics Simulation; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry*; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C480519:COMMD1 protein, human; D019006:Neural Cell Adhesion Molecules; D025801:Ubiquitin
keywords: molecular dynamics; protein electrostatics