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Int. J. Mol. Sci. 2013, 14(7), 14408-14425; doi:10.3390/ijms140714408

Dependence of Interaction Free Energy between Solutes on an External Electrostatic Field

Department of Biomedical Engineering, I-SHOU University, Kaohsiung 84001, Taiwan
Received: 24 May 2013 / Revised: 27 June 2013 / Accepted: 2 July 2013 / Published: 11 July 2013
(This article belongs to the collection Proteins and Protein-Ligand Interactions)
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Abstract

To explore the athermal effect of an external electrostatic field on the stabilities of protein conformations and the binding affinities of protein-protein/ligand interactions, the dependences of the polar and hydrophobic interactions on the external electrostatic field, −Eext, were studied using molecular dynamics (MD) simulations. By decomposing Eext into, along, and perpendicular to the direction formed by the two solutes, the effect of Eext on the interactions between these two solutes can be estimated based on the effects from these two components. Eext was applied along the direction of the electric dipole formed by two solutes with opposite charges. The attractive interaction free energy between these two solutes decreased for solutes treated as point charges. In contrast, the attractive interaction free energy between these two solutes increased, as observed by MD simulations, for Eext = 40 or 60 MV/cm. Eext was applied perpendicular to the direction of the electric dipole formed by these two solutes. The attractive interaction free energy was increased for Eext = 100 MV/cm as a result of dielectric saturation. The force on the solutes along the direction of Eext computed from MD simulations was greater than that estimated from a continuum solvent in which the solutes were treated as point charges. To explore the hydrophobic interactions, Eext was applied to a water cluster containing two neutral solutes. The repulsive force between these solutes was decreased/increased for Eext along/perpendicular to the direction of the electric dipole formed by these two solutes.
Keywords: athermal effect; potential of mean force; protein conformation; protein-protein/ligand interactions athermal effect; potential of mean force; protein conformation; protein-protein/ligand interactions
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Yang, P.-K. Dependence of Interaction Free Energy between Solutes on an External Electrostatic Field. Int. J. Mol. Sci. 2013, 14, 14408-14425.

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