An investigation of ion-pairing of alkali metal halides in aqueous solutions using the electrical conductivity and the Monte Carlo computer simulation methods

Gujt, Jure; Bešter‐Rogač, Marija; Hribar-Lee, Barbara

doi:10.1016/j.molliq.2013.09.025

Cited by 39 publications

(37 citation statements)

References 58 publications

(63 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We interpret this binding as a force-field artefact, since LiCl has a lower 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 association constant than NaCl and KCl. [50] It is likely that calculations with the Hess and van-der-Vegt parameters [40] would not have yielded this peak, though in this case Li + ions would not bind to the protein directly as they should. [37] The formation of ion-pairs implies on the structure and thermodynamics of the solutions, as discussed in.…”

Section: Protein-ion Interactionsmentioning

confidence: 99%

Protein‐ion Interactions: Simulations of Bovine Serum Albumin in Physiological Solutions of NaCl, KCl and LiCl

Becconi

Ahlstrand

Salis

et al. 2017

Israel Journal of Chemistry

View full text Add to dashboard Cite

Specific interactions that depend on the nature of electrolytes are observed when proteins and other molecules are studied by potentiometric, spectroscopic and theoretical methods at high salt concentrations. More recently, it became clear that such interactions may also be observed in solutions that can be described by the Debye‐Hückel theory, i.e., at physiological (0.1 mol dm−3) and lower concentrations. We carried out molecular dynamics simulations of bovine serum albumin in physiological solutions at T=300 and 350 K. Analysis of the simulations revealed some differences between LiCl solutions and those of NaCl and KCl. The binding of Li+ ions to the protein was associated with a negative free energy of interaction whereas much fewer Na+ and K+ ions were associated with the protein surface. Interestingly, unlike other proteins BSA does not show a preference to Na+ over K+. Quantum chemical calculations identified a significant contribution from polarisation to the hydration of Li+ and (to a lesser degree) Na+, which may indicate that polarisable force‐fields will provide more accurate results for such systems.

show abstract

Section: Protein-ion Interactionsmentioning

confidence: 99%

Protein‐ion Interactions: Simulations of Bovine Serum Albumin in Physiological Solutions of NaCl, KCl and LiCl

Becconi

Ahlstrand

Salis

et al. 2017

Israel Journal of Chemistry

View full text Add to dashboard Cite

show abstract

“…Kosmotropic cations and kosmotropic anions possess similar hydration enthalpies and DDH hyd ' 0. Their strong Coulombic interaction may survive in water keeping the ions together [65]. However, the strongest interaction between cations and anions exists if both are chaotropic.…”

Section: Law Of Matching Water Affinitiesmentioning

confidence: 99%

Proteins in Ionic Liquids: Current Status of Experiments and Simulations

Schröder¹

2017

Topics in Current Chemistry Collections

View full text Add to dashboard Cite

In the last two decades, while searching for interesting applications of ionic liquids as potent solvents, their solvation properties and their general impact on biomolecules, and in particular on proteins, gained interest. It turned out that ionic liquids are excellent solvents for protein refolding and crystallization. Biomolecules showed increased solubilities and stabilities, both operational and thermal, in ionic liquids, which also seem to prevent self-aggregation during solubilization. Biomolecules can be immobilized, e.g. in highly viscous ionic liquids, for particular biochemical processes and can be designed to some extent by the proper choice of the ionic liquid cations and anions, which can be characterized by the Hofmeister series.

show abstract

“…The interactions between Ca 2+ -X − and X − -X − pairs in solution (where X − designates Cl − or F − ), and between the ions in solution and the phosphate and hydroxyl groups of HAP were described using the Buckingham potentials developed by Rabone and de Leeuw for modeling natural apatite crystals [46]. Finally, the halide-water interactions were described using the force field parameters derived by Dang [47], because it provides an accurate description of the diffusion coefficients of halide ions, and of the dynamical and structural properties of the hydrogen bonding network [48][49][50][51][52]. The list of parameters and an assessment of the forcefield used in this work are reported in the Supplementary Materials, Sections S1 and S2.…”

Section: Interatomic Potential Modelmentioning

confidence: 99%

Molecular Dynamics Simulations of Hydroxyapatite Nanopores in Contact with Electrolyte Solutions: The Effect of Nanoconfinement and Solvated Ions on the Surface Reactivity and the Structural, Dynamical, and Vibrational Properties of Water

et al. 2017

View full text Add to dashboard Cite

Hydroxyapatite, the main mineral phase of mammalian tooth enamel and bone, grows within nanoconfined environments and in contact with aqueous solutions that are rich in ions. Hydroxyapatite nanopores of different pore sizes (20 Å ≤ H ≤ 110 Å, where H is the size of the nanopore) in contact with liquid water and aqueous electrolyte solutions (CaCl 2 (aq) and CaF 2 (aq)) were investigated using molecular dynamics simulations to quantify the effect of nanoconfinement and solvated ions on the surface reactivity and the structural and dynamical properties of water. The combined effect of solution composition and nanoconfinement significantly slows the self-diffusion coefficient of water molecules compared with bulk liquid. Analysis of the pair and angular distribution functions, distribution of hydrogen bonds, velocity autocorrelation functions, and power spectra of water shows that solution composition and nanoconfinement in particular enhance the rigidity of the water hydrogen bonding network. Calculation of the water exchange events in the coordination of calcium ions reveals that the dynamics of water molecules at the HAP-solution interface decreases substantially with the degree of confinement. Ions in solution also reduce the water dynamics at the surface calcium sites. Together, these changes in the properties of water impart an overall rigidifying effect on the solvent network and reduce the reactivity at the hydroxyapatite-solution interface. Since the process of surface-cation-dehydration governs the kinetics of the reactions occurring at mineral surfaces, such as adsorption and crystal growth, this work shows how nanoconfinement and solvation environment influence the molecular-level events surrounding the crystallization of hydroxyapatite.

show abstract

An investigation of ion-pairing of alkali metal halides in aqueous solutions using the electrical conductivity and the Monte Carlo computer simulation methods

Cited by 39 publications

References 58 publications

Protein‐ion Interactions: Simulations of Bovine Serum Albumin in Physiological Solutions of NaCl, KCl and LiCl

Protein‐ion Interactions: Simulations of Bovine Serum Albumin in Physiological Solutions of NaCl, KCl and LiCl

Proteins in Ionic Liquids: Current Status of Experiments and Simulations

Molecular Dynamics Simulations of Hydroxyapatite Nanopores in Contact with Electrolyte Solutions: The Effect of Nanoconfinement and Solvated Ions on the Surface Reactivity and the Structural, Dynamical, and Vibrational Properties of Water

Contact Info

Product

Resources

About