The Effect of External Electric Field on the Conformational Integrity of Trypsin Inhibitor: A Molecular Model Study

The folding and unfolding of proteins under exogenous perturbation is still a topic of great interest. People have conducted in-depth studies on the biological and health effects of electrostatic fields. In this study, we studied the conformational changes of trypsin inhibitor under different electric fields (low electric fields of 0.2 and 0.5-0.8 V/nm), and with the increase of the electric field, the conformational changes became more severe. Protease inhibitors are substances that can combine with enzymes to reduce the decomposition rate of substrates that enzymes act on. They are widely used in our lives and have important research value in food safety and biomedicine. Root mean square deviation (RMSD), dipole moment analysis and intermolecular hydrogen bond analysis were used to study the conformational changes of this protein.