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Ion-specific induced fluctuations and free energetics of aqueous protein hydrophobic interfaces: toward connecting to specific-ion behaviors at aqueous liquid-vapor interfaces.

ABSTRACT: We explore anion-induced interface fluctuations near protein-water interfaces using coarse-grained representations of interfaces as proposed by Willard and Chandler ( J. Phys. Chem. B 2010 , 114 , 1954 - 1958 ). We use umbrella sampling molecular dynamics to compute potentials of mean force along a reaction coordinate bridging the state where the anion is fully solvated and one where it is biased via harmonic restraints to remain at the protein-water interface. Specifically, we focus on fluctuations of an interface between water and a hydrophobic region of hydrophobin-II (HFBII), a 71 amino acid residue protein expressed by filamentous fungi and known for its ability to form hydrophobically mediated self-assemblies at interfaces such as a water/air interface. We consider the anions chloride and iodide that have been shown previously by simulations as displaying specific-ion behaviors at aqueous liquid-vapor interfaces. We find that as in the case of a pure liquid-vapor interface, at the hydrophobic protein-water interface, the larger, less charge-dense iodide anion displays a marginal interfacial stability compared with that of the smaller, more charge-dense chloride anion. Furthermore, consistent with the results at aqueous liquid-vapor interfaces, we find that iodide induces larger fluctuations of the protein-water interface than chloride.

SUBMITTER: Cui D

PROVIDER: S-EPMC4010293 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Ion-specific induced fluctuations and free energetics of aqueous protein hydrophobic interfaces: toward connecting to specific-ion behaviors at aqueous liquid-vapor interfaces.

Cui Di D Ou Shuching S Peters Eric E Patel Sandeep S

The journal of physical chemistry. B 20140417 17

We explore anion-induced interface fluctuations near protein-water interfaces using coarse-grained representations of interfaces as proposed by Willard and Chandler ( J. Phys. Chem. B 2010 , 114 , 1954 - 1958 ). We use umbrella sampling molecular dynamics to compute potentials of mean force along a reaction coordinate bridging the state where the anion is fully solvated and one where it is biased via harmonic restraints to remain at the protein-water interface. Specifically, we focus on fluctuat ...[more]

PMID: 24701961

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Project description:Endpoints density functional theory (DFT) provides a framework for calculating the excess chemical potential of a solute in solution using solvent distribution functions obtained from both physical endpoints of a hypothetical charging process which transforms the solvent density from that of the pure liquid to the solution state. In this work, the endpoints DFT equations are formulated in terms of the indirect (solvent-mediated) contribution ω(x) to the solute-solvent potential of mean force, and their connections are established with the conventional DFT expressions which are based on the use of direct correlation functions. ω actually corresponds to the free-energy cost to move a cavity particle (a tagged solvent molecule which interacts with the other solvent molecules but not the solute) from the bulk to the configuration x of a solvent molecule relative to the solute and is a suitable variable to describe the solvent effects on the solute-solvent interactions. HNC and PY type approximations are then used to integrate the DFT charging integral involved in the exact expression for the excess chemical potential. With these approximations, molecular simulations are to be performed at the two endpoints of solute insertion: pure solvent without the solute and the solution system with the fully coupled solute-solvent interaction. An endpoints method thus utilizes the ensembles of intermolecular configurations of physical interest, which are often readily accessible with MD simulations given the present computational power. To illustrate properties of the formulation, we perform simulations of model systems consisting of a cavity particle in an aqueous solution containing a spherical hydrophobic solute of three different sizes from which ω(x) and the solute chemical potential can be calculated using endpoints DFT expressions. These are compared with corresponding results obtained using the approximations needed in order to evaluate the endpoints DFT charging integral when cavity particle simulation data is not available. We analyze a new approximation (two-points quadratic HNC) to the DFT charging integral which captures the correct behavior of the cavity distributions at both endpoints of the solute insertion. The behavior of the cavity particle in simple and complex liquids plays an important role in various theoretical treatments of the solute chemical potential. For pure Lennard-Jones fluids, the free energy to bring a cavity particle from the bulk to the center of a fluid particle is negative. However, for solutes of varying size, this is not generally true for Lennard-Jones fluids or the systems studied in this work. We carry out energetic and structural analyses of the cavity particle in aqueous solution with hydrophobic solutes of varying size and discuss the results in the context of the hydrophobic effect.

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Dataset Information

Ion-specific induced fluctuations and free energetics of aqueous protein hydrophobic interfaces: toward connecting to specific-ion behaviors at aqueous liquid-vapor interfaces.

Publications

Ion-specific induced fluctuations and free energetics of aqueous protein hydrophobic interfaces: toward connecting to specific-ion behaviors at aqueous liquid-vapor interfaces.

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