Effects of an Electric Field on the Conformational Transition of the Protein: A Molecular Dynamics Simulation Study

Abstract

The effect of the electric field on the conformational properties of the protein 1BBL was investigated by molecular dynamics simulations. Our simulation results clearly capture the structural transitions of the protein sample from helix to turn or random coil conformation induced by the increasing strength of the electric field. During our analysis, we found that the conformational stability is weakened, and the protein sample is stretched as an unfolded structure when it was exposed in a sufficiently high electric field. The characteristic time when the jump occurs in the time evolution curves of root mean square deviation (RMSD) and radius of gyration Rg decreases with increasing electric strength, which demonstrates the rapidly conformational transition that occurs. The number of intra-protein hydrogen bonds, which is the key factor for stabilizing the protein structure, is related to the overall size of the protein. The value of the dipole moment and characteristic time are both influenced by the strength, but are independent of the direction of the external field. The protein sample becomes rotated with the electric field direction. These conclusions provide a theoretical realization of understanding the protein conformational transition in an electric field and the guidance for anticipative applications.

Membrane Chaperoning of a Thylakoid Protease Whose Structural Stability Is Modified by the Protonmotive Force

“…Additionally, the apparent lack of major chaperones in the thylakoid lumen (Kieselbach and Schröder, 2003;Peltier et al, 2002;Schubert et al, 2002) may necessitate other means to stabilize proteins under periods of stress. While not discussed here, the electrical component of the pmf can also influence protein functions (Bekard and Dunstan, 2014;Jiang et al, 2019). Overall, we suggest our work has the potential to prompt and inform future discussions about the role of lipids and electrochemical gradients in protein structure and function.…”

“…Hamsanathan and Musser (2018) recently considered explicitly that the native environment of a protein embedded in an energetic membrane would necessarily include the pmf. Indeed, an influence of an electric field on protein structural stability has been observed experimentally (Bekard and Dunstan, 2014) and by simulations (Jiang et al, 2019). Extramembranous effects of the pmf necessarily include the pH values in the flanking compartments, i.e., the thylakoid lumen in the case of Plsp1.…”

Local Surface Electric Field’s Effect on Adsorbed Proteins’ Orientation

“…Another study shows that the application of external fields of even higher magnitudes can dramatically disrupt the secondary structure of another small peptide (V3-loop), from a native β-sheet to α-helix, through the rearrangement of amide dipole moments [66]. A recent simulation study shows that the application of strong external electric fields on the α-helix dominant dihydrolipoamide dehydrogenase induces the despiralization of the helical structure to turns and random coils [67]. However, when it comes to much larger proteins, it has been shown that upon the application of external electric fields as low as 8 V/cm on the antibody immunoglobulin G (IgG), it is observed via AFM that the protein molecules are aligned in the direction of the applied field [68].…”

Pulsed electric fields induce modulation of protein liquid–liquid phase separation

“…where n is the total number of protein atoms, q i is the charge of the atom i, r i is the directional vector of each atom. 45 Based on this correlation, we investigated the influence of EFs on the phase behaviors of proteins with different electric dipole moments. Results obtained are shown in ESI, † Fig.…”

“…carbon nanotubes, nanowires and conducting polymers. 37,38 Experiments analyzing the effect of EFs on biological systems and biomolecular suspensions focused till now predominantly on investigating the impact of EFs on protein crystallization, 25,26,39,40 protein dynamics, 41 protein conformation/structure, [42][43][44][45][46][47] and cellular morphologies. 48 Experimental efforts to understand the influence of EFs on the formation of protein LDCs have only rarely been performed.…”