Resumen
Proteins undergo a series of conformational changes when affected by the applied electric field, which changes their functions and properties. The conformational changes in proteins in various electric fields are different due to their internal structures. This study simulates the molecular dynamics of proteins in different amounts and directions of electric fields with gromacs software. According to the root mean square deviation, hydrogen bond, dipole moment, and solvent accessible surface area, it is proved that the conformation change in proteins is more drastic under the simultaneous action of multiple electric fields under various directions, and different fragments unfold with divergent electric fields combined, which is of great importance to control protein function, improve biochemical research and production efficiency in the food and drug safety field.