## 3 Results and Discussions
### Hydrogen Bond Analysis  
Proteins have a secondary structure because the peptide backbone hovers or folds according to a certain law in space, which is manifested as the \(\alpha\)-helix, \(\beta\)-folding, \(\beta\)-corner, and \(\Omega\)-rings and other structural conformations. Hydrogen bonds are molecular forces stronger than van der Waals' forces formed via the covalent bonding of hydrogen atoms and electronegativity atoms in proteins with secondary structures. Since changes in the secondary structure of proteins lead to changes in hydrogen bonds inside and outside the proteins, this paper provides lateral proofs of conformational changes in proteins by analyzing and comparing the changes in the number and length of hydrogen bonds inside the proteins and between proteins and water after an applied electric field [33]. As can be seen from Figure 4, the number of hydrogen bonds inside the reference group (310 K, 0 v/nm) protein without an electric field is stable at around 120. The number of hydrogen bonds inside the protein decreases significantly after the electrostatic field is applied [24], which indicates that the original internal structure of the protein changes under the action of the electric field, and the hydrogen bond between the secondary structure begins to break. The change in the number of hydrogen bonds between the protein and water can be observed in Figure 5, and it is not difficult to find that the number of hydrogen bonds in this part changed and the number of hydrogen bonds in the protein changed in a complementary relationship. Taking the simultaneous application of the 0.5 v/nm electric field in the x, y, and z axes as an example, the number of intermolecular hydrogen bonds of proteins decreased to the minimum when the simulation started at about 10 ns. Correspondingly, the number of hydrogen bonds between protein molecules and water molecules increased to the maximum at about 10 ns; that is, the number of hydrogen bonds inside the protein decreased, and the hydrogen bond increased with the water because more hydrogen bonds are formed with the water molecules after the hydrogen bond breaks under the action of the electric field. In addition, the electric field's strength also has an impact on the speed at which hydrogen bonds break and form. From Figure 4, it can be found that the drop time of the number of hydrogen bonds when applying a 0.5 v/nm electric field in one direction is around 30 ns. As the number of electric fields increases, the strength of the combined field becomes larger, the time for the hydrogen bond change in  
Figure 3: Protein dipole moment curves under different numbers and directional electric fields. the protein is also shortened, and the decline time of the number of hydrogen bonds inside the protein is only about 20 ns when the electric field is applied to the two sides, while the decline time when the electric field is applied at the same time in the direction of the x, y, z coordinate axis is only 5-10 ns, and it can be seen that the strength of the electric field has a great impact on the conformational change rate of the protein. Figure 4: (**a,b**) Represents the curves of change in the number and length of hydrogen bonds inside proteins under different amounts and directional electric fields. Figure 5: The curves of the change in the number of hydrogen bonds between proteins and water under different amount and directional electric fields. To accurately describe the conformational changes in proteins, we then calculated and analyzed the number of hydrogen bonds between the three residues selected above and the water and the hydrogen bond length inside the residues to obtain Figure 6. It was then found that the number of hydrogen bonds between residues 61 and 88 and water under the action of the electric field increased significantly and, combined with the above parameter analysis, it can be seen that the secondary structure of this area changed, and the contact area with water increased while more hydrogen bonds were formed with water molecules [34].